메뉴 건너뛰기




Volumn 30, Issue 12, 2016, Pages 3942-3960

Who watches the watchmen? Regulation of the expression and activity of sirtuins

Author keywords

Deacetylation; MiRNA; Post translational modification; SIRT; Transcriptional regulation

Indexed keywords

MICRORNA; SIRTUIN; SIRTUIN 1; SIRTUIN 2; SIRTUIN 3; SIRTUIN 4; SIRTUIN 5; SIRTUIN 6; SIRTUIN 7; NICOTINAMIDE ADENINE DINUCLEOTIDE;

EID: 85002376289     PISSN: 08926638     EISSN: 15306860     Source Type: Journal    
DOI: 10.1096/fj.201600410RR     Document Type: Article
Times cited : (73)

References (240)
  • 1
    • 0034677535 scopus 로고    scopus 로고
    • Transcriptional silencing and longevity protein Sir2 is an NADdependent histone deacetylase
    • Imai, S., Armstrong, C.M., Kaeberlein, M., and Guarente, L. (2000) Transcriptional silencing and longevity protein Sir2 is an NADdependent histone deacetylase. Nature 403, 795-800
    • (2000) Nature , vol.403 , pp. 795-800
    • Imai, S.1    Armstrong, C.M.2    Kaeberlein, M.3    Guarente, L.4
  • 4
    • 84996553972 scopus 로고    scopus 로고
    • Identification of 'erasers' for lysine crotonylated histone marks using a chemical proteomics approach
    • Bao, X., Wang, Y., Li, X., Li, X.-M., Liu, Z., Yang, T., Wong, C. F., Zhang, J., Hao, Q., and Li, X.D. (2014) Identification of 'erasers' for lysine crotonylated histone marks using a chemical proteomics approach. eLife 3, 3
    • (2014) ELife , vol.3 , pp. 3
    • Bao, X.1    Wang, Y.2    Li, X.3    Li, X.-M.4    Liu, Z.5    Yang, T.6    Wong, C.F.7    Zhang, J.8    Hao, Q.9    Li, X.D.10
  • 5
    • 84926628054 scopus 로고    scopus 로고
    • Mitochondrial sirtuins and their relationships with metabolic disease and cancer
    • Kumar, S., and Lombard, D. B. (2015) Mitochondrial sirtuins and their relationships with metabolic disease and cancer. Antioxid. Redox Signal. 22, 1060-1077
    • (2015) Antioxid. Redox Signal. , vol.22 , pp. 1060-1077
    • Kumar, S.1    Lombard, D.B.2
  • 6
    • 33750887809 scopus 로고    scopus 로고
    • The role of NAD+ dependent histone deacetylases (sirtuins) in ageing
    • Trapp, J., and Jung, M. (2006) The role of NAD+ dependent histone deacetylases (sirtuins) in ageing. Curr. Drug Targets 7, 1553-1560
    • (2006) Curr. Drug Targets , vol.7 , pp. 1553-1560
    • Trapp, J.1    Jung, M.2
  • 7
    • 0033214237 scopus 로고    scopus 로고
    • The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms
    • Kaeberlein, M., McVey, M., and Guarente, L. (1999) The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms. Genes Dev. 13, 2570-2580
    • (1999) Genes Dev. , vol.13 , pp. 2570-2580
    • Kaeberlein, M.1    McVey, M.2    Guarente, L.3
  • 8
    • 84960153337 scopus 로고    scopus 로고
    • The role of sirtuins in aging and age-related diseases
    • Wątroba, M., and Szukiewicz, D. (2016) The role of sirtuins in aging and age-related diseases. Adv. Med. Sci. 61, 52-62
    • (2016) Adv. Med. Sci. , vol.61 , pp. 52-62
    • Wątroba, M.1    Szukiewicz, D.2
  • 9
    • 17144424946 scopus 로고    scopus 로고
    • SIRT3, a mitochondrial sirtuin deacetylase, regulatesmitochondrial function and thermogenesis in brown adipocytes
    • Shi, T., Wang, F., Stieren, E., and Tong, Q. (2005) SIRT3, a mitochondrial sirtuin deacetylase, regulatesmitochondrial function and thermogenesis in brown adipocytes. J. Biol. Chem. 280, 13560-13567
    • (2005) J. Biol. Chem. , vol.280 , pp. 13560-13567
    • Shi, T.1    Wang, F.2    Stieren, E.3    Tong, Q.4
  • 11
    • 84937524287 scopus 로고    scopus 로고
    • Regulation of NAD biosynthetic enzymes modulates NAD-sensing processes to shape mammalian cell physiology under varying biological cues
    • Ruggieri, S., Orsomando, G., Sorci, L., and Raffaelli, N. (2015) Regulation of NAD biosynthetic enzymes modulates NAD-sensing processes to shape mammalian cell physiology under varying biological cues. Biochim. Biophys. Acta 1854, 1138-1149
    • (2015) Biochim. Biophys. Acta , vol.1854 , pp. 1138-1149
    • Ruggieri, S.1    Orsomando, G.2    Sorci, L.3    Raffaelli, N.4
  • 12
    • 84956956644 scopus 로고    scopus 로고
    • Dynamics of NAD-metabolism: Everything but constant
    • Opitz, C. A., and Heiland, I. (2015) Dynamics of NAD-metabolism: everything but constant. Biochem. Soc. Trans. 43, 1127-1132
    • (2015) Biochem. Soc. Trans. , vol.43 , pp. 1127-1132
    • Opitz, C.A.1    Heiland, I.2
  • 13
    • 84949036094 scopus 로고    scopus 로고
    • + in aging, metabolism, and neurodegeneration
    • + in aging, metabolism, and neurodegeneration. Science 350, 1208-1213
    • (2015) Science , vol.350 , pp. 1208-1213
    • Verdin, E.1
  • 16
    • 34250365395 scopus 로고    scopus 로고
    • Nucleocytoplasmic shuttling of the NAD+-dependent histone deacetylase SIRT1
    • Tanno, M., Sakamoto, J., Miura, T., Shimamoto, K., and Horio, Y. (2007) Nucleocytoplasmic shuttling of the NAD+-dependent histone deacetylase SIRT1. J. Biol. Chem. 282, 6823-6832
    • (2007) J. Biol. Chem. , vol.282 , pp. 6823-6832
    • Tanno, M.1    Sakamoto, J.2    Miura, T.3    Shimamoto, K.4    Horio, Y.5
  • 17
    • 0035863153 scopus 로고    scopus 로고
    • A cytosolic NAD-dependent deacetylase, Hst2p, canmodulate nucleolar and telomeric silencing in yeast
    • Perrod, S., Cockell, M. M., Laroche, T., Renauld, H., Ducrest, A. L., Bonnard, C., and Gasser, S. M. (2001) A cytosolic NAD-dependent deacetylase, Hst2p, canmodulate nucleolar and telomeric silencing in yeast. EMBO J. 20, 197-209
    • (2001) EMBO J. , vol.20 , pp. 197-209
    • Perrod, S.1    Cockell, M.M.2    Laroche, T.3    Renauld, H.4    Ducrest, A.L.5    Bonnard, C.6    Gasser, S.M.7
  • 19
    • 0037108799 scopus 로고    scopus 로고
    • SIRT3, a human SIR2 homologue, is an NADdependent deacetylase localized to mitochondria
    • Onyango, P., Celic, I., McCaffery, J. M., Boeke, J. D., and Feinberg, A. P. (2002) SIRT3, a human SIR2 homologue, is an NADdependent deacetylase localized to mitochondria. Proc. Natl. Acad. Sci. USA 99, 13653-13658
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 13653-13658
    • Onyango, P.1    Celic, I.2    McCaffery, J.M.3    Boeke, J.D.4    Feinberg, A.P.5
  • 20
    • 84871852995 scopus 로고    scopus 로고
    • SIRT3 functions in the nucleus in the control of stress-related gene expression
    • Iwahara, T., Bonasio, R., Narendra, V., and Reinberg, D. (2012) SIRT3 functions in the nucleus in the control of stress-related gene expression. Mol. Cell. Biol. 32, 5022-5034
    • (2012) Mol. Cell. Biol. , vol.32 , pp. 5022-5034
    • Iwahara, T.1    Bonasio, R.2    Narendra, V.3    Reinberg, D.4
  • 21
    • 26244436281 scopus 로고    scopus 로고
    • Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins
    • Michishita, E., Park, J. Y., Burneskis, J. M., Barrett, J. C., and Horikawa, I. (2005) Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins. Mol. Biol. Cell 16, 4623-4635
    • (2005) Mol. Biol. Cell , vol.16 , pp. 4623-4635
    • Michishita, E.1    Park, J.Y.2    Burneskis, J.M.3    Barrett, J.C.4    Horikawa, I.5
  • 25
    • 33744466971 scopus 로고    scopus 로고
    • Mammalian Sir2 homolog SIRT7 is an activator of RNA polymerase I transcription
    • Ford, E., Voit, R., Liszt, G., Magin, C., Grummt, I., and Guarente, L. (2006) Mammalian Sir2 homolog SIRT7 is an activator of RNA polymerase I transcription. Genes Dev. 20, 1075-1080
    • (2006) Genes Dev. , vol.20 , pp. 1075-1080
    • Ford, E.1    Voit, R.2    Liszt, G.3    Magin, C.4    Grummt, I.5    Guarente, L.6
  • 26
    • 84940976163 scopus 로고    scopus 로고
    • Sirtuin regulation in aging and injury
    • Poulose, N., and Raju, R. (2015) Sirtuin regulation in aging and injury. Biochim. Biophys. Acta 1852, 2442-2455
    • (2015) Biochim. Biophys. Acta , vol.1852 , pp. 2442-2455
    • Poulose, N.1    Raju, R.2
  • 27
    • 77949887506 scopus 로고    scopus 로고
    • Mammalian sirtuins: Biological insights and disease relevance
    • Haigis, M. C., and Sinclair, D. A. (2010) Mammalian sirtuins: biological insights and disease relevance. Annu. Rev. Pathol. 5, 253-295
    • (2010) Annu. Rev. Pathol. , vol.5 , pp. 253-295
    • Haigis, M.C.1    Sinclair, D.A.2
  • 28
    • 84887428122 scopus 로고    scopus 로고
    • The roles of SIRT1 in cancer
    • Lin, Z., and Fang, D. (2013) The roles of SIRT1 in cancer. Genes Cancer 4, 97-104
    • (2013) Genes Cancer , vol.4 , pp. 97-104
    • Lin, Z.1    Fang, D.2
  • 31
    • 84896498683 scopus 로고    scopus 로고
    • SIRT1 gene polymorphisms affect the protein expression in cardiovascular diseases
    • Kilic, U., Gok, O., Bacaksiz, A., Izmirli, M., Elibol-Can, B., and Uysal, O. (2014) SIRT1 gene polymorphisms affect the protein expression in cardiovascular diseases. PLoS One 9, e90428
    • (2014) PLoS One , vol.9 , pp. e90428
    • Kilic, U.1    Gok, O.2    Bacaksiz, A.3    Izmirli, M.4    Elibol-Can, B.5    Uysal, O.6
  • 32
    • 84868317415 scopus 로고    scopus 로고
    • The interactive effect of SIRT1 promoter region polymorphism on type 2 diabetes susceptibility in the North Indian population
    • Rai, E., Sharma, S., Kaul, S., Jain, K., Matharoo, K., Bhanwer, A. S., and Bamezai, R. N. K. (2012) The interactive effect of SIRT1 promoter region polymorphism on type 2 diabetes susceptibility in the North Indian population. PLoS One 7, e48621
    • (2012) PLoS One , vol.7 , pp. e48621
    • Rai, E.1    Sharma, S.2    Kaul, S.3    Jain, K.4    Matharoo, K.5    Bhanwer, A.S.6    Bamezai, R.N.K.7
  • 33
    • 84862300236 scopus 로고    scopus 로고
    • Genetic analysis of SIRT1 gene promoter in sporadic Parkinson's disease
    • Zhang, A., Wang, H., Qin, X., Pang, S., and Yan, B. (2012) Genetic analysis of SIRT1 gene promoter in sporadic Parkinson's disease. Biochem. Biophys. Res. Commun. 422, 693-696
    • (2012) Biochem. Biophys. Res. Commun. , vol.422 , pp. 693-696
    • Zhang, A.1    Wang, H.2    Qin, X.3    Pang, S.4    Yan, B.5
  • 35
    • 84901855770 scopus 로고    scopus 로고
    • Functional sequence variants within the SIRT1 gene promoter in indirect inguinal hernia
    • Han, Q., Zhang, Y., Li, W., Fan, H., Xing, Q., Pang, S., and Yan, B. (2014) Functional sequence variants within the SIRT1 gene promoter in indirect inguinal hernia. Gene 546, 1-5
    • (2014) Gene , vol.546 , pp. 1-5
    • Han, Q.1    Zhang, Y.2    Li, W.3    Fan, H.4    Xing, Q.5    Pang, S.6    Yan, B.7
  • 37
    • 77952288176 scopus 로고    scopus 로고
    • Fasting promotes the expression of SIRT1, an NAD+ -dependent protein deacetylase, via activation of PPARalpha in mice
    • Hayashida, S., Arimoto, A., Kuramoto, Y., Kozako, T., Honda, S., Shimeno, H., and Soeda, S. (2010) Fasting promotes the expression of SIRT1, an NAD+ -dependent protein deacetylase, via activation of PPARalpha in mice. Mol. Cell. Biochem. 339, 285-292
    • (2010) Mol. Cell. Biochem. , vol.339 , pp. 285-292
    • Hayashida, S.1    Arimoto, A.2    Kuramoto, Y.3    Kozako, T.4    Honda, S.5    Shimeno, H.6    Soeda, S.7
  • 39
    • 78649852533 scopus 로고    scopus 로고
    • SIRT1 is regulated by a PPARγ-SIRT1negative feedback loop associated with senescence
    • Han, L., Zhou, R., Niu, J., McNutt, M. A., Wang, P., and Tong, T. (2010) SIRT1 is regulated by a PPARγ-SIRT1negative feedback loop associated with senescence. Nucleic Acids Res. 38, 7458-7471
    • (2010) Nucleic Acids Res. , vol.38 , pp. 7458-7471
    • Han, L.1    Zhou, R.2    Niu, J.3    McNutt, M.A.4    Wang, P.5    Tong, T.6
  • 40
    • 84940236618 scopus 로고    scopus 로고
    • Sirt1 and Sirt6mediate beneficial effects of rosiglitazone on hepatic lipid accumulation
    • Yang, S. J., Choi, J.M., Chang, E., Park, S.W., and Park, C.-Y. (2014) Sirt1 and Sirt6mediate beneficial effects of rosiglitazone on hepatic lipid accumulation. PLoS One 9, e105456
    • (2014) PLoS One , vol.9 , pp. e105456
    • Yang, S.J.1    Choi, J.M.2    Chang, E.3    Park, S.W.4    Park, C.-Y.5
  • 41
    • 79953152333 scopus 로고    scopus 로고
    • FoxO1 mediates an auto feedback loop regulating SIRT1 expression
    • Xiong, S., Salazar, G., Patrushev, N., and Alexander, R. W. (2011) FoxO1 mediates an auto feedback loop regulating SIRT1 expression. J. Biol. Chem. 286, 5289-5299
    • (2011) J. Biol. Chem. , vol.286 , pp. 5289-5299
    • Xiong, S.1    Salazar, G.2    Patrushev, N.3    Alexander, R.W.4
  • 43
    • 10844236451 scopus 로고    scopus 로고
    • Nutrient availability regulates SIRT1 through a forkhead-dependent pathway
    • Nemoto, S., Fergusson, M. M., and Finkel, T. (2004) Nutrient availability regulates SIRT1 through a forkhead-dependent pathway. Science 306, 2105-2108
    • (2004) Science , vol.306 , pp. 2105-2108
    • Nemoto, S.1    Fergusson, M.M.2    Finkel, T.3
  • 44
    • 80052022281 scopus 로고    scopus 로고
    • Thereduction of SIRT1in livers of oldmice leads toimpaired body homeostasis and to inhibition of liver proliferation
    • Jin, J., Iakova, P., Jiang, Y., Medrano, E. E., and Timchenko, N. A. (2011) Thereduction of SIRT1in livers of oldmice leads toimpaired body homeostasis and to inhibition of liver proliferation. Hepatology 54, 989-998
    • (2011) Hepatology , vol.54 , pp. 989-998
    • Jin, J.1    Iakova, P.2    Jiang, Y.3    Medrano, E.E.4    Timchenko, N.A.5
  • 45
    • 77950538806 scopus 로고    scopus 로고
    • C/EBPalpha regulates SIRT1 expression during adipogenesis
    • Jin, Q., Zhang, F., Yan, T., Liu, Z., Wang, C., Ge, X., and Zhai, Q. (2010) C/EBPalpha regulates SIRT1 expression during adipogenesis. Cell Res. 20, 470-479
    • (2010) Cell Res. , vol.20 , pp. 470-479
    • Jin, Q.1    Zhang, F.2    Yan, T.3    Liu, Z.4    Wang, C.5    Ge, X.6    Zhai, Q.7
  • 47
    • 0035913911 scopus 로고    scopus 로고
    • Negative control of p53 by Sir2alpha promotes cell survival under stress
    • Luo, J., Nikolaev, A. Y., Imai, S., Chen, D., Su, F., Shiloh, A., Guarente, L., and Gu, W. (2001) Negative control of p53 by Sir2alpha promotes cell survival under stress. Cell 107, 137-148
    • (2001) Cell , vol.107 , pp. 137-148
    • Luo, J.1    Nikolaev, A.Y.2    Imai, S.3    Chen, D.4    Su, F.5    Shiloh, A.6    Guarente, L.7    Gu, W.8
  • 49
    • 84892534814 scopus 로고    scopus 로고
    • Transcription factor NFκB regulates the expression of the histone deacetylase SIRT1
    • Katto, J., Engel, N., Abbas, W., Herbein, G., and Mahlknecht, U. (2013) Transcription factor NFκB regulates the expression of the histone deacetylase SIRT1. Clin. Epigenetics 5, 11
    • (2013) Clin. Epigenetics , vol.5 , pp. 11
    • Katto, J.1    Engel, N.2    Abbas, W.3    Herbein, G.4    Mahlknecht, U.5
  • 50
    • 77954218572 scopus 로고    scopus 로고
    • Involvement of the p65/RelA subunit of NF-kappaB in TNF-alpha-induced SIRT1 expression in vascular smooth muscle cells
    • Zhang, H.-N., Li, L., Gao, P., Chen, H.-Z., Zhang, R., Wei, Y.-S., Liu, D.-P., and Liang, C.-C. (2010) Involvement of the p65/RelA subunit of NF-kappaB in TNF-alpha-induced SIRT1 expression in vascular smooth muscle cells. Biochem. Biophys. Res. Commun. 397, 569-575
    • (2010) Biochem. Biophys. Res. Commun. , vol.397 , pp. 569-575
    • Zhang, H.-N.1    Li, L.2    Gao, P.3    Chen, H.-Z.4    Zhang, R.5    Wei, Y.-S.6    Liu, D.-P.7    Liang, C.-C.8
  • 51
    • 3242719545 scopus 로고    scopus 로고
    • Modulation of NF-kappaB dependent transcription and cell survival by the SIRT1 deacetylase
    • Yeung, F., Hoberg, J. E., Ramsey, C. S., Keller, M. D., Jones, D. R., Frye, R. A., and Mayo, M. W. (2004) Modulation of NF-kappaB dependent transcription and cell survival by the SIRT1 deacetylase. EMBO J. 23, 2369-2380
    • (2004) EMBO J. , vol.23 , pp. 2369-2380
    • Yeung, F.1    Hoberg, J.E.2    Ramsey, C.S.3    Keller, M.D.4    Jones, D.R.5    Frye, R.A.6    Mayo, M.W.7
  • 53
    • 84868107900 scopus 로고    scopus 로고
    • An autoregulatory loop reverts the mechanosensitive Sirt1 induction by EGR1 in skeletal muscle cells
    • Pardo, P. S., and Boriek, A.M. (2012) An autoregulatory loop reverts the mechanosensitive Sirt1 induction by EGR1 in skeletal muscle cells. Aging (Albany, N.Y.) 4, 456-461
    • (2012) Aging (Albany, N.Y.) , vol.4 , pp. 456-461
    • Pardo, P.S.1    Boriek, A.M.2
  • 56
    • 54249107873 scopus 로고    scopus 로고
    • The ups and downs of SIRT1
    • Kwon, H.-S., and Ott, M. (2008) The ups and downs of SIRT1. Trends Biochem. Sci. 33, 517-525
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 517-525
    • Kwon, H.-S.1    Ott, M.2
  • 57
    • 27544434763 scopus 로고    scopus 로고
    • Tumor suppressor HIC1 directly regulates SIRT1 to modulatep53-dependent DNA-damage responses
    • Chen, W. Y., Wang, D.H., Yen, R. C., Luo, J., Gu, W., and Baylin, S. B. (2005) Tumor suppressor HIC1 directly regulates SIRT1 to modulatep53-dependent DNA-damage responses. Cell 123, 437-448
    • (2005) Cell , vol.123 , pp. 437-448
    • Chen, W.Y.1    Wang, D.H.2    Yen, R.C.3    Luo, J.4    Gu, W.5    Baylin, S.B.6
  • 58
    • 77955499804 scopus 로고    scopus 로고
    • Sirtuin 1 modulates cellular responses to hypoxia by deacetylating hypoxia-inducible factor 1alpha
    • Lim, J.-H., Lee, Y.-M., Chun, Y.-S., Chen, J., Kim, J.-E., and Park, J.-W. (2010) Sirtuin 1 modulates cellular responses to hypoxia by deacetylating hypoxia-inducible factor 1alpha. Mol. Cell 38, 864-878
    • (2010) Mol. Cell , vol.38 , pp. 864-878
    • Lim, J.-H.1    Lee, Y.-M.2    Chun, Y.-S.3    Chen, J.4    Kim, J.-E.5    Park, J.-W.6
  • 60
    • 79954609893 scopus 로고    scopus 로고
    • Hypoxia increases sirtuin1 expressionin ahypoxia-inducible factor-dependent manner
    • Chen, R., Dioum, E. M., Hogg, R. T., Gerard, R. D., and Garcia, J.A. (2011) Hypoxia increases sirtuin1 expressionin ahypoxia-inducible factor-dependent manner. J. Biol. Chem. 286, 13869-13878
    • (2011) J. Biol. Chem. , vol.286 , pp. 13869-13878
    • Chen, R.1    Dioum, E.M.2    Hogg, R.T.3    Gerard, R.D.4    Garcia, J.A.5
  • 62
    • 84904395742 scopus 로고    scopus 로고
    • Molecular pathways: Harnessing E2F1 regulation for prosenescence therapy in p53-defective cancer cells
    • Laine, A., and Westermarck, J. (2014) Molecular pathways: harnessing E2F1 regulation for prosenescence therapy in p53-defective cancer cells. Clin. Cancer Res. 20, 3644-3650
    • (2014) Clin. Cancer Res. , vol.20 , pp. 3644-3650
    • Laine, A.1    Westermarck, J.2
  • 63
    • 84896984997 scopus 로고    scopus 로고
    • FoxM1 regulates Sirt1 expression in glioma cells
    • Zhu, G.-Y., Shi, B.-Z., and Li, Y. (2014) FoxM1 regulates Sirt1 expression in glioma cells. Eur. Rev. Med. Pharmacol. Sci. 18, 205-211
    • (2014) Eur. Rev. Med. Pharmacol. Sci. , vol.18 , pp. 205-211
    • Zhu, G.-Y.1    Shi, B.-Z.2    Li, Y.3
  • 64
    • 84857181300 scopus 로고    scopus 로고
    • Activating transcription factor 4 confers a multidrug resistance phenotype to gastric cancer cells through transactivation of SIRT1 expression
    • Zhu, H., Xia, L., Zhang, Y., Wang, H., Xu, W., Hu, H., Wang, J., Xin, J., Gang, Y., Sha, S., Xu, B., Fan, D., Nie, Y., and Wu, K. (2012) Activating transcription factor 4 confers a multidrug resistance phenotype to gastric cancer cells through transactivation of SIRT1 expression. PLoS One 7, e31431
    • (2012) PLoS One , vol.7 , pp. e31431
    • Zhu, H.1    Xia, L.2    Zhang, Y.3    Wang, H.4    Xu, W.5    Hu, H.6    Wang, J.7    Xin, J.8    Gang, Y.9    Sha, S.10    Xu, B.11    Fan, D.12    Nie, Y.13    Wu, K.14
  • 65
    • 58249088751 scopus 로고    scopus 로고
    • MicroRNAs: Target recognition and regulatory functions
    • Bartel, D. P. (2009) MicroRNAs: target recognition and regulatory functions. Cell 136, 215-233
    • (2009) Cell , vol.136 , pp. 215-233
    • Bartel, D.P.1
  • 67
    • 84866314843 scopus 로고    scopus 로고
    • MicroRNA regulation of SIRT1
    • Yamakuchi, M. (2012) MicroRNA regulation of SIRT1. Front. Physiol. 3, 68
    • (2012) Front. Physiol. , vol.3 , pp. 68
    • Yamakuchi, M.1
  • 69
    • 84941309370 scopus 로고    scopus 로고
    • MiR-9a-5p regulates proliferation and migration of hepatic stellate cells under pressure through inhibition of Sirt1
    • Qi, F., Hu, J.-F., Liu, B.-H., Wu, C.-Q., Yu, H.-Y., Yao, D.-K., and Zhu, L. (2015) MiR-9a-5p regulates proliferation and migration of hepatic stellate cells under pressure through inhibition of Sirt1. World J. Gastroenterol. 21, 9900-9915
    • (2015) World J. Gastroenterol. , vol.21 , pp. 9900-9915
    • Qi, F.1    Hu, J.-F.2    Liu, B.-H.3    Wu, C.-Q.4    Yu, H.-Y.5    Yao, D.-K.6    Zhu, L.7
  • 70
    • 84954065789 scopus 로고    scopus 로고
    • MicroRNA-22 functions as a tumor suppressor by targeting SIRT1 in renal cell carcinoma
    • Zhang, S., Zhang, D., Yi, C., Wang, Y., Wang, H., and Wang, J. (2015) MicroRNA-22 functions as a tumor suppressor by targeting SIRT1 in renal cell carcinoma. Oncol. Rep. 35, 559-567
    • (2015) Oncol. Rep. , vol.35 , pp. 559-567
    • Zhang, S.1    Zhang, D.2    Yi, C.3    Wang, Y.4    Wang, H.5    Wang, J.6
  • 72
    • 79952742806 scopus 로고    scopus 로고
    • Increased expression of miR-34a and miR-93 in rat liver during aging, and their impact on the expression of Mgst1 and Sirt1
    • Li, N., Muthusamy, S., Liang, R., Sarojini, H., and Wang, E. (2011) Increased expression of miR-34a and miR-93 in rat liver during aging, and their impact on the expression of Mgst1 and Sirt1. Mech. Ageing Dev. 132, 75-85
    • (2011) Mech. Ageing Dev. , vol.132 , pp. 75-85
    • Li, N.1    Muthusamy, S.2    Liang, R.3    Sarojini, H.4    Wang, E.5
  • 76
    • 84904157844 scopus 로고    scopus 로고
    • Metformin induces microRNA-34a to downregulate the Sirt1/Pgc-1α/Nrf2 pathway, leading to increased susceptibility of wild-type p53 cancer cells to oxidative stress and therapeutic agents
    • Do, M.T., Kim, H.G., Choi, J.H., and Jeong, H.G. (2014) Metformin induces microRNA-34a to downregulate the Sirt1/Pgc-1α/Nrf2 pathway, leading to increased susceptibility of wild-type p53 cancer cells to oxidative stress and therapeutic agents. Free Radic. Biol. Med. 74, 21-34
    • (2014) Free Radic. Biol. Med. , vol.74 , pp. 21-34
    • Do, M.T.1    Kim, H.G.2    Choi, J.H.3    Jeong, H.G.4
  • 77
    • 84964694199 scopus 로고    scopus 로고
    • Metformin and rapamycin reduce pancreatic cancer growth in obese prediabetic mice by distinct microRNA-regulated mechanisms
    • Cifarelli, V., Lashinger, L.M., Devlin, K. L., Dunlap, S.M., Huang, J., Kaaks, R., Pollak, M. N., and Hursting, S. D. (2015) Metformin and rapamycin reduce pancreatic cancer growth in obese prediabetic mice by distinct microRNA-regulated mechanisms. Diabetes 64, 1632-1642
    • (2015) Diabetes , vol.64 , pp. 1632-1642
    • Cifarelli, V.1    Lashinger, L.M.2    Devlin, K.L.3    Dunlap, S.M.4    Huang, J.5    Kaaks, R.6    Pollak, M.N.7    Hursting, S.D.8
  • 79
    • 84959420544 scopus 로고    scopus 로고
    • Molecular interplay between microRNA-34a and sirtuin1 in hyperglycaemia-mediated impaired angiogenesis in endothelial cells: Effects of metformin
    • Arunachalam, G., Lakshmanan, A. P., Samuel, S.M., Triggle, C., and Ding, H. (2015) Molecular interplay between microRNA-34a and sirtuin1 in hyperglycaemia-mediated impaired angiogenesis in endothelial cells: effects of metformin. J. Pharmacol. Exp. Ther. 356, 314-323
    • (2015) J. Pharmacol. Exp. Ther. , vol.356 , pp. 314-323
    • Arunachalam, G.1    Lakshmanan, A.P.2    Samuel, S.M.3    Triggle, C.4    Ding, H.5
  • 81
    • 84891485491 scopus 로고    scopus 로고
    • MicroRNA-126 inhibits osteosarcoma cells proliferation by targeting Sirt1
    • Xu, J.-Q., Liu, P., Si, M.-J., and Ding, X.-Y. (2013) MicroRNA-126 inhibits osteosarcoma cells proliferation by targeting Sirt1. Tumour Biol. 34, 3871-3877
    • (2013) Tumour Biol. , vol.34 , pp. 3871-3877
    • Xu, J.-Q.1    Liu, P.2    Si, M.-J.3    Ding, X.-Y.4
  • 82
    • 85027938704 scopus 로고    scopus 로고
    • MiR-132 inhibits expression of SIRT1 and induces pro-inflammatory processes of vascular endothelial inflammation through blockade of the SREBP-1c metabolic pathway
    • Zhang, L., Huang, D., Wang, Q., Shen, D., Wang, Y., Chen, B., Zhang, J., and Gai, L. (2014) MiR-132 inhibits expression of SIRT1 and induces pro-inflammatory processes of vascular endothelial inflammation through blockade of the SREBP-1c metabolic pathway. Cardiovasc. Drugs Ther. 28, 303-311
    • (2014) Cardiovasc. Drugs Ther. , vol.28 , pp. 303-311
    • Zhang, L.1    Huang, D.2    Wang, Q.3    Shen, D.4    Wang, Y.5    Chen, B.6    Zhang, J.7    Gai, L.8
  • 83
    • 70350436694 scopus 로고    scopus 로고
    • MicroRNA 132 regulates nutritional stress-induced chemokine production through repression of SirT1
    • Strum, J. C., Johnson, J. H., Ward, J., Xie, H., Feild, J., Hester, A., Alford, A., and Waters, K. M. (2009) MicroRNA 132 regulates nutritional stress-induced chemokine production through repression of SirT1. Mol. Endocrinol. 23, 1876-1884
    • (2009) Mol. Endocrinol. , vol.23 , pp. 1876-1884
    • Strum, J.C.1    Johnson, J.H.2    Ward, J.3    Xie, H.4    Feild, J.5    Hester, A.6    Alford, A.7    Waters, K.M.8
  • 84
    • 84936985198 scopus 로고    scopus 로고
    • MiR-138 promotes smooth muscle cells proliferation and migration in db/db mice through down-regulation of SIRT1
    • Xu, J., Li, L., Yun, H. F., and Han, Y. S. (2015) MiR-138 promotes smooth muscle cells proliferation and migration in db/db mice through down-regulation of SIRT1. Biochem. Biophys. Res. Commun. 463, 1159-1164
    • (2015) Biochem. Biophys. Res. Commun. , vol.463 , pp. 1159-1164
    • Xu, J.1    Li, L.2    Yun, H.F.3    Han, Y.S.4
  • 85
    • 84884941624 scopus 로고    scopus 로고
    • MicroRNA-146b promotes adipogenesis by suppressing the SIRT1-FOXO1 cascade
    • Ahn, J., Lee, H., Jung, C. H., Jeon, T. I., and Ha, T. Y. (2013) MicroRNA-146b promotes adipogenesis by suppressing the SIRT1-FOXO1 cascade. EMBO Mol. Med. 5, 1602-1612
    • (2013) EMBO Mol. Med. , vol.5 , pp. 1602-1612
    • Ahn, J.1    Lee, H.2    Jung, C.H.3    Jeon, T.I.4    Ha, T.Y.5
  • 87
    • 84898599871 scopus 로고    scopus 로고
    • MiR-195 regulates SIRT1-mediated changes in diabetic retinopathy
    • Mortuza, R., Feng, B., and Chakrabarti, S. (2014) miR-195 regulates SIRT1-mediated changes in diabetic retinopathy. Diabetologia 57, 1037-1046
    • (2014) Diabetologia , vol.57 , pp. 1037-1046
    • Mortuza, R.1    Feng, B.2    Chakrabarti, S.3
  • 88
    • 84888004362 scopus 로고    scopus 로고
    • MiR-199a-5p promotes migration and tube formation of human cytomegalovirus-infected endothelial cells through downregulation of SIRT1 and eNOS
    • Zhang, S., Liu, L., Wang, R., Tuo, H., Guo, Y., Yi, L., Wang, J., and Wang, D. (2013) MiR-199a-5p promotes migration and tube formation of human cytomegalovirus-infected endothelial cells through downregulation of SIRT1 and eNOS. Arch. Virol. 158, 2443-2452
    • (2013) Arch. Virol. , vol.158 , pp. 2443-2452
    • Zhang, S.1    Liu, L.2    Wang, R.3    Tuo, H.4    Guo, Y.5    Yi, L.6    Wang, J.7    Wang, D.8
  • 89
    • 65249185780 scopus 로고    scopus 로고
    • Downregulation of miR-199a derepresses hypoxiainducible factor-1alpha and Sirtuin 1 and recapitulates hypoxia preconditioning in cardiac myocytes
    • Rane, S., He, M., Sayed, D., Vashistha, H., Malhotra, A., Sadoshima, J., Vatner, D. E., Vatner, S. F., and Abdellatif, M. (2009) Downregulation of miR-199a derepresses hypoxiainducible factor-1alpha and Sirtuin 1 and recapitulates hypoxia preconditioning in cardiac myocytes. Circ. Res. 104, 879-886
    • (2009) Circ. Res. , vol.104 , pp. 879-886
    • Rane, S.1    He, M.2    Sayed, D.3    Vashistha, H.4    Malhotra, A.5    Sadoshima, J.6    Vatner, D.E.7    Vatner, S.F.8    Abdellatif, M.9
  • 90
    • 84930021925 scopus 로고    scopus 로고
    • MicroRNA-204 inhibits proliferation, migration, invasion and epithelial-mesenchymal transition in osteosarcoma cells via targeting Sirtuin 1
    • Shi, Y., Huang, J., Zhou, J., Liu, Y., Fu, X., Li, Y., Yin, G., and Wen, J. (2015) MicroRNA-204 inhibits proliferation, migration, invasion and epithelial-mesenchymal transition in osteosarcoma cells via targeting Sirtuin 1. Oncol. Rep. 34, 399-406
    • (2015) Oncol. Rep. , vol.34 , pp. 399-406
    • Shi, Y.1    Huang, J.2    Zhou, J.3    Liu, Y.4    Fu, X.5    Li, Y.6    Yin, G.7    Wen, J.8
  • 91
    • 84878894582 scopus 로고    scopus 로고
    • MiR-204 down regulates SIRT1 and reverts SIRT1-induced epithelial-mesenchymal transition, anoikis resistance and invasion in gastric cancer cells
    • Zhang, L., Wang, X., and Chen, P. (2013) MiR-204 down regulates SIRT1 and reverts SIRT1-induced epithelial-mesenchymal transition, anoikis resistance and invasion in gastric cancer cells. BMC Cancer 13, 290
    • (2013) BMC Cancer , vol.13 , pp. 290
    • Zhang, L.1    Wang, X.2    Chen, P.3
  • 92
    • 84946615576 scopus 로고    scopus 로고
    • MicroRNA-212 negatively regulates starvation induced autophagy in prostate cancer cells by inhibiting SIRT1 and is a modulator of angiogenesis and cellular senescence
    • Ramalinga, M., Roy, A., Srivastava, A., Bhattarai, A., Harish, V., Suy, S., Collins, S., and Kumar, D. (2015) MicroRNA-212 negatively regulates starvation induced autophagy in prostate cancer cells by inhibiting SIRT1 and is a modulator of angiogenesis and cellular senescence. Oncotarget 6, 34446-34457
    • (2015) Oncotarget , vol.6 , pp. 34446-34457
    • Ramalinga, M.1    Roy, A.2    Srivastava, A.3    Bhattarai, A.4    Harish, V.5    Suy, S.6    Collins, S.7    Kumar, D.8
  • 94
    • 82155163830 scopus 로고    scopus 로고
    • MiR-520c and miR-373 upregulate MMP9 expression by targeting mTOR and SIRT1, and activate the Ras/Raf/MEK/Erk signaling pathway and NF-κB factor in human fibrosarcoma cells
    • Liu, P., and Wilson, M. J. (2012) miR-520c and miR-373 upregulate MMP9 expression by targeting mTOR and SIRT1, and activate the Ras/Raf/MEK/Erk signaling pathway and NF-κB factor in human fibrosarcoma cells. J. Cell. Physiol. 227, 867-876
    • (2012) J. Cell. Physiol. , vol.227 , pp. 867-876
    • Liu, P.1    Wilson, M.J.2
  • 95
    • 84907195200 scopus 로고    scopus 로고
    • MicroRNA-449 suppresses proliferation of hepatoma cell lines through blockade lipid metabolic pathway related to SIRT1
    • Zhang, H., Feng, Z., Huang, R., Xia, Z., Xiang, G., and Zhang, J. (2014) MicroRNA-449 suppresses proliferation of hepatoma cell lines through blockade lipid metabolic pathway related to SIRT1. Int. J. Oncol. 45, 2143-2152
    • (2014) Int. J. Oncol. , vol.45 , pp. 2143-2152
    • Zhang, H.1    Feng, Z.2    Huang, R.3    Xia, Z.4    Xiang, G.5    Zhang, J.6
  • 97
    • 84940890937 scopus 로고    scopus 로고
    • Ectopic expression of miR-494 inhibited the proliferation, invasion and chemoresistance of pancreatic cancer by regulating SIRT1 and c-Myc
    • Liu, Y., Li, X., Zhu, S., Zhang, J. G., Yang, M., Qin, Q., Deng, S. C., Wang, B., Tian, K., Liu, L., Niu, Y., Wang, C. Y., and Zhao, G. (2015) Ectopic expression of miR-494 inhibited the proliferation, invasion and chemoresistance of pancreatic cancer by regulating SIRT1 and c-Myc. Gene Ther. 22, 729-738
    • (2015) Gene Ther. , vol.22 , pp. 729-738
    • Liu, Y.1    Li, X.2    Zhu, S.3    Zhang, J.G.4    Yang, M.5    Qin, Q.6    Deng, S.C.7    Wang, B.8    Tian, K.9    Liu, L.10    Niu, Y.11    Wang, C.Y.12    Zhao, G.13
  • 98
    • 84951566980 scopus 로고    scopus 로고
    • MiR-543 promotes gastric cancer cell proliferation by targeting SIRT1
    • Li, J., Dong, G., Wang, B., Gao, W., and Yang, Q. (2015) miR-543 promotes gastric cancer cell proliferation by targeting SIRT1. Biochem. Biophys. Res. Commun. 469, 15-21
    • (2015) Biochem. Biophys. Res. Commun. , vol.469 , pp. 15-21
    • Li, J.1    Dong, G.2    Wang, B.3    Gao, W.4    Yang, Q.5
  • 100
    • 84928139602 scopus 로고    scopus 로고
    • The p53/miR-34a/SIRT1 positive feedback loop in quercetin-induced apoptosis
    • Lou, G., Liu, Y., Wu, S., Xue, J., Yang, F., Fu, H., Zheng, M., and Chen, Z. (2015) The p53/miR-34a/SIRT1 positive feedback loop in quercetin-induced apoptosis. Cell. Physiol. Biochem. 35, 2192-2202
    • (2015) Cell. Physiol. Biochem. , vol.35 , pp. 2192-2202
    • Lou, G.1    Liu, Y.2    Wu, S.3    Xue, J.4    Yang, F.5    Fu, H.6    Zheng, M.7    Chen, Z.8
  • 101
    • 84874960373 scopus 로고    scopus 로고
    • Mutual inhibition between miR-34a and SIRT1 contributes to regulation of DNA double-strand break repair
    • Xu, M., Lu, L., Mao, B., Lü, X., Wu, X., Li, L., and Liu, D. (2012) Mutual inhibition between miR-34a and SIRT1 contributes to regulation of DNA double-strand break repair. Chin. Sci. Bull. 58, 979-985
    • (2012) Chin. Sci. Bull. , vol.58 , pp. 979-985
    • Xu, M.1    Lu, L.2    Mao, B.3    Lü, X.4    Wu, X.5    Li, L.6    Liu, D.7
  • 102
    • 0035496607 scopus 로고    scopus 로고
    • Rescuing the function of mutant p53
    • Bullock, A. N., and Fersht, A. R. (2001) Rescuing the function of mutant p53. Nat. Rev. Cancer 1, 68-76
    • (2001) Nat. Rev. Cancer , vol.1 , pp. 68-76
    • Bullock, A.N.1    Fersht, A.R.2
  • 103
    • 84903697938 scopus 로고    scopus 로고
    • SIRT5 is under the control of PGC-1α and AMPK and is involved in regulation of mitochondrial energy metabolism
    • Buler, M., Aatsinki, S.-M., Izzi, V., Uusimaa, J., and Hakkola, J. (2014) SIRT5 is under the control of PGC-1α and AMPK and is involved in regulation of mitochondrial energy metabolism. FASEB J. 28, 3225-3237
    • (2014) FASEB J. , vol.28 , pp. 3225-3237
    • Buler, M.1    Aatsinki, S.-M.2    Izzi, V.3    Uusimaa, J.4    Hakkola, J.5
  • 104
    • 84935009342 scopus 로고    scopus 로고
    • A metabolic stress-inducible miR-34a-HNF4α pathway regulates lipid and lipoprotein metabolism
    • Xu, Y., Zalzala, M., Xu, J., Li, Y., Yin, L., and Zhang, Y. (2015) A metabolic stress-inducible miR-34a-HNF4α pathway regulates lipid and lipoprotein metabolism. Nat. Commun. 6, 7466
    • (2015) Nat. Commun. , vol.6 , pp. 7466
    • Xu, Y.1    Zalzala, M.2    Xu, J.3    Li, Y.4    Yin, L.5    Zhang, Y.6
  • 105
    • 84928036633 scopus 로고    scopus 로고
    • Sirt7 promotes gastric cancer growth and inhibits apoptosis by epigenetically inhibiting miR-34a
    • Zhang, S., Chen, P., Huang, Z., Hu, X., Chen, M., Hu, S., Hu, Y., and Cai, T. (2015) Sirt7 promotes gastric cancer growth and inhibits apoptosis by epigenetically inhibiting miR-34a. Sci. Rep. 5, 9787
    • (2015) Sci. Rep. , vol.5 , pp. 9787
    • Zhang, S.1    Chen, P.2    Huang, Z.3    Hu, X.4    Chen, M.5    Hu, S.6    Hu, Y.7    Cai, T.8
  • 107
    • 84864667383 scopus 로고    scopus 로고
    • Regulation of sirtuin function by posttranslational modifications
    • Flick, F., and Lüscher, B. (2012) Regulation of sirtuin function by posttranslational modifications. Front. Pharmacol. 3, 29
    • (2012) Front. Pharmacol. , vol.3 , pp. 29
    • Flick, F.1    Lüscher, B.2
  • 108
    • 84874228973 scopus 로고    scopus 로고
    • The ways and means that fine tune Sirt1 activity
    • Revollo, J. R., and Li, X. (2013) The ways and means that fine tune Sirt1 activity. Trends Biochem. Sci. 38, 160-167
    • (2013) Trends Biochem. Sci. , vol.38 , pp. 160-167
    • Revollo, J.R.1    Li, X.2
  • 111
    • 53649100104 scopus 로고    scopus 로고
    • JNK2-dependent regulation of SIRT1 protein stability
    • Ford, J., Ahmed, S., Allison, S., Jiang, M., and Milner, J. (2008) JNK2-dependent regulation of SIRT1 protein stability. Cell Cycle 7, 3091-3097
    • (2008) Cell Cycle , vol.7 , pp. 3091-3097
    • Ford, J.1    Ahmed, S.2    Allison, S.3    Jiang, M.4    Milner, J.5
  • 112
    • 84926429973 scopus 로고    scopus 로고
    • Ubiquitinated sirtuin 1 (SIRT1) function is modulated during DNA damage-induced cell death and survival
    • Peng, L., Yuan, Z., Li, Y., Ling, H., Izumi, V., Fang, B., Fukasawa, K., Koomen, J., Chen, J., and Seto, E. (2015) Ubiquitinated sirtuin 1 (SIRT1) function is modulated during DNA damage-induced cell death and survival. J. Biol. Chem. 290, 8904-8912
    • (2015) J. Biol. Chem. , vol.290 , pp. 8904-8912
    • Peng, L.1    Yuan, Z.2    Li, Y.3    Ling, H.4    Izumi, V.5    Fang, B.6    Fukasawa, K.7    Koomen, J.8    Chen, J.9    Seto, E.10
  • 113
    • 35748962613 scopus 로고    scopus 로고
    • SIRT1 sumoylation regulates its deacetylase activity and cellular response to genotoxic stress
    • Yang, Y., Fu, W., Chen, J., Olashaw, N., Zhang, X., Nicosia, S. V., Bhalla, K., and Bai, W. (2007) SIRT1 sumoylation regulates its deacetylase activity and cellular response to genotoxic stress. Nat. Cell Biol. 9, 1253-1262
    • (2007) Nat. Cell Biol. , vol.9 , pp. 1253-1262
    • Yang, Y.1    Fu, W.2    Chen, J.3    Olashaw, N.4    Zhang, X.5    Nicosia, S.V.6    Bhalla, K.7    Bai, W.8
  • 114
    • 77956180402 scopus 로고    scopus 로고
    • SIRT1 is a redox-sensitive deacetylase that is post-translationally modified by oxidants and carbonyl stress
    • Caito, S., Rajendrasozhan, S., Cook, S., Chung, S., Yao, H., Friedman, A.E., Brookes, P. S., and Rahman, I. (2010) SIRT1 is a redox-sensitive deacetylase that is post-translationally modified by oxidants and carbonyl stress. FASEB J. 24, 3145-3159
    • (2010) FASEB J. , vol.24 , pp. 3145-3159
    • Caito, S.1    Rajendrasozhan, S.2    Cook, S.3    Chung, S.4    Yao, H.5    Friedman, A.E.6    Brookes, P.S.7    Rahman, I.8
  • 116
    • 84861461517 scopus 로고    scopus 로고
    • USP22 antagonizes p53 transcriptional activation by deubiquitinating Sirt1 to suppress cell apoptosis and is required for mouse embryonic development
    • Lin, Z., Yang, H., Kong, Q., Li, J., Lee, S. M., Gao, B., Dong, H., Wei, J., Song, J., Zhang, D. D., and Fang, D. (2012) USP22 antagonizes p53 transcriptional activation by deubiquitinating Sirt1 to suppress cell apoptosis and is required for mouse embryonic development. Mol. Cell 46, 484-494
    • (2012) Mol. Cell , vol.46 , pp. 484-494
    • Lin, Z.1    Yang, H.2    Kong, Q.3    Li, J.4    Lee, S.M.5    Gao, B.6    Dong, H.7    Wei, J.8    Song, J.9    Zhang, D.D.10    Fang, D.11
  • 117
    • 4944245398 scopus 로고    scopus 로고
    • Human SirT1 interacts with histone H1 and promotes formation of facultative heterochromatin
    • Vaquero, A., Scher, M., Lee, D., Erdjument-Bromage, H., Tempst, P., and Reinberg, D. (2004) Human SirT1 interacts with histone H1 and promotes formation of facultative heterochromatin. Mol. Cell 16, 93-105
    • (2004) Mol. Cell , vol.16 , pp. 93-105
    • Vaquero, A.1    Scher, M.2    Lee, D.3    Erdjument-Bromage, H.4    Tempst, P.5    Reinberg, D.6
  • 118
    • 77951225449 scopus 로고    scopus 로고
    • DYRK1A and DYRK3 promote cell survival through phosphorylation and activation of SIRT1
    • Guo, X., Williams, J.G., Schug, T. T., and Li, X. (2010) DYRK1A and DYRK3 promote cell survival through phosphorylation and activation of SIRT1. J. Biol. Chem. 285, 13223-13232
    • (2010) J. Biol. Chem. , vol.285 , pp. 13223-13232
    • Guo, X.1    Williams, J.G.2    Schug, T.T.3    Li, X.4
  • 119
    • 45549102566 scopus 로고    scopus 로고
    • Regulation of SIRT1 protein levels by nutrient availability
    • Kanfi, Y., Peshti, V., Gozlan, Y.M., Rathaus, M., Gil, R., and Cohen, H. Y. (2008) Regulation of SIRT1 protein levels by nutrient availability. FEBS Lett. 582, 2417-2423
    • (2008) FEBS Lett. , vol.582 , pp. 2417-2423
    • Kanfi, Y.1    Peshti, V.2    Gozlan, Y.M.3    Rathaus, M.4    Gil, R.5    Cohen, H.Y.6
  • 120
    • 0033600176 scopus 로고    scopus 로고
    • Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activity
    • Frye, R. A. (1999) Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activity. Biochem. Biophys. Res. Commun. 260, 273-279
    • (1999) Biochem. Biophys. Res. Commun. , vol.260 , pp. 273-279
    • Frye, R.A.1
  • 121
    • 0037291214 scopus 로고    scopus 로고
    • The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase
    • North, B. J., Marshall, B. L., Borra, M. T., Denu, J.M., and Verdin, E. (2003) The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase. Mol. Cell 11, 437-444
    • (2003) Mol. Cell , vol.11 , pp. 437-444
    • North, B.J.1    Marshall, B.L.2    Borra, M.T.3    Denu, J.M.4    Verdin, E.5
  • 122
    • 84923337675 scopus 로고    scopus 로고
    • Efficient demyristoylase activity of SIRT2 revealed by kinetic and structural studies
    • Teng, Y.-B., Jing, H., Aramsangtienchai, P., He, B., Khan, S., Hu, J., Lin, H., and Hao, Q. (2015) Efficient demyristoylase activity of SIRT2 revealed by kinetic and structural studies. Sci. Rep. 5, 8529
    • (2015) Sci. Rep. , vol.5 , pp. 8529
    • Teng, Y.-B.1    Jing, H.2    Aramsangtienchai, P.3    He, B.4    Khan, S.5    Hu, J.6    Lin, H.7    Hao, Q.8
  • 123
    • 34447626095 scopus 로고    scopus 로고
    • SIRT2 deacetylates FOXO3a in response to oxidative stress and caloric restriction
    • Wang, F., Nguyen, M., Qin, F. X. F., and Tong, Q. (2007) SIRT2 deacetylates FOXO3a in response to oxidative stress and caloric restriction. Aging Cell 6, 505-514
    • (2007) Aging Cell , vol.6 , pp. 505-514
    • Wang, F.1    Nguyen, M.2    Qin, F.X.F.3    Tong, Q.4
  • 124
    • 33847793039 scopus 로고    scopus 로고
    • Sirtuin 2, amammalian homolog of yeast silent information regulator-2 longevity regulator, is an oligodendroglial protein that decelerates cell differentiation through deacetylating alpha-tubulin
    • Li, W., Zhang, B., Tang, J., Cao, Q., Wu, Y., Wu, C., Guo, J., Ling, E.-A., and Liang, F. (2007) Sirtuin 2, amammalian homolog of yeast silent information regulator-2 longevity regulator, is an oligodendroglial protein that decelerates cell differentiation through deacetylating alpha-tubulin. J. Neurosci. 27, 2606-2616
    • (2007) J. Neurosci. , vol.27 , pp. 2606-2616
    • Li, W.1    Zhang, B.2    Tang, J.3    Cao, Q.4    Wu, Y.5    Wu, C.6    Guo, J.7    Ling, E.-A.8    Liang, F.9
  • 126
    • 84946227815 scopus 로고    scopus 로고
    • Emerging role of sirtuin 2 in the regulation of mammalian metabolism
    • Gomes, P., Outeiro, T. F., and Cavadas, C. (2015) Emerging role of sirtuin 2 in the regulation of mammalian metabolism. Trends Pharmacol. Sci. 36, 756-768
    • (2015) Trends Pharmacol. Sci. , vol.36 , pp. 756-768
    • Gomes, P.1    Outeiro, T.F.2    Cavadas, C.3
  • 127
    • 84949057909 scopus 로고    scopus 로고
    • Acetylation of glucokinase regulatory protein decreases glucose metabolism by suppressing glucokinase activity
    • Park, J.-M., Kim, T.-H., Jo, S.-H., Kim, M.-Y., and Ahn, Y.-H. (2015) Acetylation of glucokinase regulatory protein decreases glucose metabolism by suppressing glucokinase activity. Sci. Rep. 5, 17395
    • (2015) Sci. Rep. , vol.5 , pp. 17395
    • Park, J.-M.1    Kim, T.-H.2    Jo, S.-H.3    Kim, M.-Y.4    Ahn, Y.-H.5
  • 128
    • 79959906869 scopus 로고    scopus 로고
    • Acetylation regulates gluconeogenesis by promoting PEPCK1 degradation via recruiting the UBR5 ubiquitin ligase
    • Jiang, W., Wang, S., Xiao, M., Lin, Y., Zhou, L., Lei, Q., Xiong, Y., Guan, K.-L., and Zhao, S. (2011) Acetylation regulates gluconeogenesis by promoting PEPCK1 degradation via recruiting the UBR5 ubiquitin ligase. Mol. Cell 43, 33-44
    • (2011) Mol. Cell , vol.43 , pp. 33-44
    • Jiang, W.1    Wang, S.2    Xiao, M.3    Lin, Y.4    Zhou, L.5    Lei, Q.6    Xiong, Y.7    Guan, K.-L.8    Zhao, S.9
  • 130
    • 64049089450 scopus 로고    scopus 로고
    • SIRT2 suppresses adipocyte differentiation by deacetylating FOXO1 and enhancing FOXO1's repressive interaction with PPARgamma
    • Wang, F., and Tong, Q. (2009) SIRT2 suppresses adipocyte differentiation by deacetylating FOXO1 and enhancing FOXO1's repressive interaction with PPARgamma. Mol. Biol. Cell 20, 801-808
    • (2009) Mol. Biol. Cell , vol.20 , pp. 801-808
    • Wang, F.1    Tong, Q.2
  • 132
    • 84886686038 scopus 로고    scopus 로고
    • Activation of the protein deacetylase SIRT6 by long-chain fatty acids and widespread deacylation by mammalian sirtuins
    • Feldman, J. L., Baeza, J., and Denu, J. M. (2013) Activation of the protein deacetylase SIRT6 by long-chain fatty acids and widespread deacylation by mammalian sirtuins. J. Biol. Chem. 288, 31350-31356
    • (2013) J. Biol. Chem. , vol.288 , pp. 31350-31356
    • Feldman, J.L.1    Baeza, J.2    Denu, J.M.3
  • 137
    • 84859447698 scopus 로고    scopus 로고
    • The role of sirtuin 2 activation by nicotinamide phosphoribosyl transferase in the aberrant proliferation and survival of myeloid leukemia cells
    • Dan, L., Klimenkova, O., Klimiankou, M., Klusman, J. H., van den Heuvel-Eibrink, M. M., Reinhardt, D., Welte, K., and Skokowa, J. (2012) The role of sirtuin 2 activation by nicotinamide phosphoribosyl transferase in the aberrant proliferation and survival of myeloid leukemia cells. Haematologica 97, 551-559
    • (2012) Haematologica , vol.97 , pp. 551-559
    • Dan, L.1    Klimenkova, O.2    Klimiankou, M.3    Klusman, J.H.4    Van Den-Heuvel-Eibrink, M.M.5    Reinhardt, D.6    Welte, K.7    Skokowa, J.8
  • 141
    • 84870380891 scopus 로고    scopus 로고
    • α-Tubulin acetylation from the inside out
    • Al-Bassam, J., and Corbett, K. D. (2012) α-Tubulin acetylation from the inside out. Proc. Natl. Acad. Sci. USA 109, 19515-19516
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 19515-19516
    • Al-Bassam, J.1    Corbett, K.D.2
  • 143
    • 54549101258 scopus 로고    scopus 로고
    • Cyclin-dependent kinases and cell-cycle transitions: Does one fit all?
    • Hochegger, H., Takeda, S., and Hunt, T. (2008) Cyclin-dependent kinases and cell-cycle transitions: does one fit all? Nat. Rev. Mol. Cell Biol. 9, 910-916
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 910-916
    • Hochegger, H.1    Takeda, S.2    Hunt, T.3
  • 144
    • 34547098165 scopus 로고    scopus 로고
    • Mitotic regulation of SIRT2 by cyclin-dependent kinase 1-dependent phosphorylation
    • North, B. J., and Verdin, E. (2007) Mitotic regulation of SIRT2 by cyclin-dependent kinase 1-dependent phosphorylation. J. Biol. Chem. 282, 19546-19555
    • (2007) J. Biol. Chem. , vol.282 , pp. 19546-19555
    • North, B.J.1    Verdin, E.2
  • 146
    • 83455218635 scopus 로고    scopus 로고
    • Sirt2 is a novel in vivo downstream target of Nkx2.2 and enhances oligodendroglial cell differentiation
    • Ji, S., Doucette, J. R., and Nazarali, A. J. (2011) Sirt2 is a novel in vivo downstream target of Nkx2.2 and enhances oligodendroglial cell differentiation. J. Mol. Cell Biol. 3, 351-359
    • (2011) J. Mol. Cell Biol. , vol.3 , pp. 351-359
    • Ji, S.1    Doucette, J.R.2    Nazarali, A.J.3
  • 147
    • 84903792981 scopus 로고    scopus 로고
    • Tissue-specific deregulation of selected HDACs characterizes ALS progression in mouse models: Pharmacological characterization of SIRT1 and SIRT2 pathways
    • Valle, C., Salvatori, I., Gerbino, V., Rossi, S., Palamiuc, L., René, F., and Carrì, M. T. (2014) Tissue-specific deregulation of selected HDACs characterizes ALS progression in mouse models: pharmacological characterization of SIRT1 and SIRT2 pathways. Cell Death Dis. 5, e1296
    • (2014) Cell Death Dis. , vol.5 , pp. e1296
    • Valle, C.1    Salvatori, I.2    Gerbino, V.3    Rossi, S.4    Palamiuc, L.5    René, F.6    Carrì, M.T.7
  • 148
    • 84933074270 scopus 로고    scopus 로고
    • Acupuncture may exert its therapeutic effect through microRNA-339/Sirt2/NFκB/FOXO1 axis
    • Wang, J.-Y., Li, H., Ma, C.-M., Wang, J.-L., Lai, X.-S., and Zhou, S.-F. (2015) Acupuncture may exert its therapeutic effect through microRNA-339/Sirt2/NFκB/FOXO1 axis. BioMed Res. Int. 2015, 428591
    • (2015) BioMed Res. Int. , vol.2015 , pp. 428591
    • Wang, J.-Y.1    Li, H.2    Ma, C.-M.3    Wang, J.-L.4    Lai, X.-S.5    Zhou, S.-F.6
  • 154
    • 9344237090 scopus 로고    scopus 로고
    • Distinct pathways of insulinregulated versus diabetes-regulated gene expression: An in vivo analysis in MIRKOmice
    • Yechoor, V. K., Patti, M.-E., Ueki, K., Laustsen, P. G., Saccone, R., Rauniyar, R., and Kahn, C. R. (2004) Distinct pathways of insulinregulated versus diabetes-regulated gene expression: an in vivo analysis in MIRKOmice. Proc. Natl. Acad. Sci. USA 101, 16525-16530
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 16525-16530
    • Yechoor, V.K.1    Patti, M.-E.2    Ueki, K.3    Laustsen, P.G.4    Saccone, R.5    Rauniyar, R.6    Kahn, C.R.7
  • 155
    • 84872448285 scopus 로고    scopus 로고
    • High glucose induced alteration of SIRTs in endothelial cells causes rapid aging in a p300 and FOXO regulated pathway
    • Mortuza, R., Chen, S., Feng, B., Sen, S., and Chakrabarti, S. (2013) High glucose induced alteration of SIRTs in endothelial cells causes rapid aging in a p300 and FOXO regulated pathway. PLoS One 8, e54514
    • (2013) PLoS One , vol.8 , pp. e54514
    • Mortuza, R.1    Chen, S.2    Feng, B.3    Sen, S.4    Chakrabarti, S.5
  • 156
    • 77955347446 scopus 로고    scopus 로고
    • Sirtuin 3, a new target of PGC-1alpha, plays an important role in the suppression of ROS and mitochondrial biogenesis
    • Kong, X., Wang, R., Xue, Y., Liu, X., Zhang, H., Chen, Y., Fang, F., and Chang, Y. (2010) Sirtuin 3, a new target of PGC-1alpha, plays an important role in the suppression of ROS and mitochondrial biogenesis. PLoS One 5, e11707
    • (2010) PLoS One , vol.5 , pp. e11707
    • Kong, X.1    Wang, R.2    Xue, Y.3    Liu, X.4    Zhang, H.5    Chen, Y.6    Fang, F.7    Chang, Y.8
  • 157
    • 79955768567 scopus 로고    scopus 로고
    • Peroxisome proliferatoractivated receptor-gamma coactivator-1alpha controls transcription of the Sirt3 gene, an essential component of the thermogenic brown adipocyte phenotype
    • Giralt, A., Hondares, E., Villena, J.A., Ribas, F., Díaz-Delfín, J., Giralt, M., Iglesias, R., and Villarroya, F. (2011) Peroxisome proliferatoractivated receptor-gamma coactivator-1alpha controls transcription of the Sirt3 gene, an essential component of the thermogenic brown adipocyte phenotype. J. Biol. Chem. 286, 16958-16966
    • (2011) J. Biol. Chem. , vol.286 , pp. 16958-16966
    • Giralt, A.1    Hondares, E.2    Villena, J.A.3    Ribas, F.4    Díaz-Delfín, J.5    Giralt, M.6    Iglesias, R.7    Villarroya, F.8
  • 160
    • 45549103553 scopus 로고    scopus 로고
    • PGC-1-related coactivator complexes with HCF-1 and NRF-2beta in mediating NRF-2(GABP)-dependent respiratory gene expression
    • Vercauteren, K., Gleyzer, N., and Scarpulla, R. C. (2008) PGC-1-related coactivator complexes with HCF-1 and NRF-2beta in mediating NRF-2(GABP)-dependent respiratory gene expression. J. Biol. Chem. 283, 12102-12111
    • (2008) J. Biol. Chem. , vol.283 , pp. 12102-12111
    • Vercauteren, K.1    Gleyzer, N.2    Scarpulla, R.C.3
  • 162
    • 84869221105 scopus 로고    scopus 로고
    • Metformin reduces hepatic expression of SIRT3, themitochondrial deacetylase controlling energy metabolism
    • Buler, M., Aatsinki, S.-M., Izzi, V., and Hakkola, J. (2012) Metformin reduces hepatic expression of SIRT3, themitochondrial deacetylase controlling energy metabolism. PLoS One 7, e49863
    • (2012) PLoS One , vol.7 , pp. e49863
    • Buler, M.1    Aatsinki, S.-M.2    Izzi, V.3    Hakkola, J.4
  • 163
    • 84945494393 scopus 로고    scopus 로고
    • Dihydromyricetin improves skeletal muscle insulin sensitivity by inducing autophagy via the AMPK-PGC-1α-Sirt3 signaling pathway
    • Shi, L., Zhang, T., Zhou, Y., Zeng, X., Ran, L., Zhang, Q., Zhu, J., and Mi, M. (2015) Dihydromyricetin improves skeletal muscle insulin sensitivity by inducing autophagy via the AMPK-PGC-1α-Sirt3 signaling pathway. Endocrine 50, 378-389
    • (2015) Endocrine , vol.50 , pp. 378-389
    • Shi, L.1    Zhang, T.2    Zhou, Y.3    Zeng, X.4    Ran, L.5    Zhang, Q.6    Zhu, J.7    Mi, M.8
  • 164
    • 84940020988 scopus 로고    scopus 로고
    • Melatonin protects hepatocytes against bile acid-induced mitochondrial oxidative stress via the AMPK-SIRT3-SOD2 pathway
    • Chen, Y., Qing, W., Sun, M., Lv, L., Guo, D., and Jiang, Y. (2015) Melatonin protects hepatocytes against bile acid-induced mitochondrial oxidative stress via the AMPK-SIRT3-SOD2 pathway. Free Radic. Res. 49, 1275-1284
    • (2015) Free Radic. Res. , vol.49 , pp. 1275-1284
    • Chen, Y.1    Qing, W.2    Sun, M.3    Lv, L.4    Guo, D.5    Jiang, Y.6
  • 165
    • 84866912720 scopus 로고    scopus 로고
    • Salvianolic acid A protects the peripheral nerve function in diabetic rats through regulation of the AMPK-PGC1α-Sirt3 axis
    • Yu, X., Zhang, L., Yang, X., Huang, H., Huang, Z., Shi, L., Zhang, H., and Du, G. (2012) Salvianolic acid A protects the peripheral nerve function in diabetic rats through regulation of the AMPK-PGC1α-Sirt3 axis. Molecules 17, 11216-11228
    • (2012) Molecules , vol.17 , pp. 11216-11228
    • Yu, X.1    Zhang, L.2    Yang, X.3    Huang, H.4    Huang, Z.5    Shi, L.6    Zhang, H.7    Du, G.8
  • 167
    • 84898859036 scopus 로고    scopus 로고
    • Metformin ameliorates insulin resistance in L6 rat skeletal muscle cells through upregulation of SIRT3
    • Song, Y., Shi, J., Wu, Y., Han, C., Zou, J., Shi, Y., and Liu, Z. (2014) Metformin ameliorates insulin resistance in L6 rat skeletal muscle cells through upregulation of SIRT3. Chin. Med. J. (Engl.) 127, 1523-1529
    • (2014) Chin. Med. J. (Engl.) , vol.127 , pp. 1523-1529
    • Song, Y.1    Shi, J.2    Wu, Y.3    Han, C.4    Zou, J.5    Shi, Y.6    Liu, Z.7
  • 168
    • 84939260692 scopus 로고    scopus 로고
    • Mitochondrial Sirt3 expression is decreased in APP/PS1 double transgenic mouse model of Alzheimer's disease
    • Yang, W., Zou, Y., Zhang, M., Zhao, N., Tian, Q., Gu, M., Liu, W., Shi, R., Lü, Y., and Yu, W. (2015) Mitochondrial Sirt3 expression is decreased in APP/PS1 double transgenic mouse model of Alzheimer's disease. Neurochem. Res. 40, 1576-1582
    • (2015) Neurochem. Res. , vol.40 , pp. 1576-1582
    • Yang, W.1    Zou, Y.2    Zhang, M.3    Zhao, N.4    Tian, Q.5    Gu, M.6    Liu, W.7    Shi, R.8    Lü, Y.9    Yu, W.10
  • 172
    • 65249091951 scopus 로고    scopus 로고
    • Investigating the ADP-ribosyltransferase activity of sirtuins with NAD analogues and 32PNAD
    • Du, J., Jiang, H., and Lin, H. (2009) Investigating the ADP-ribosyltransferase activity of sirtuins with NAD analogues and 32PNAD. Biochemistry 48, 2878-2890
    • (2009) Biochemistry , vol.48 , pp. 2878-2890
    • Du, J.1    Jiang, H.2    Lin, H.3
  • 179
    • 79952117379 scopus 로고    scopus 로고
    • Calorie restrictiononinsulin resistance and expression of SIRT1 and SIRT4 in rats
    • Chen, Y.-R., Fang, S.-R., Fu, Y.-C., Zhou, X.-H., Xu, M.-Y., and Xu, W.-C. (2010) Calorie restrictiononinsulin resistance and expression of SIRT1 and SIRT4 in rats. Biochem. Cell Biol. 88, 715-722
    • (2010) Biochem. Cell Biol. , vol.88 , pp. 715-722
    • Chen, Y.-R.1    Fang, S.-R.2    Fu, Y.-C.3    Zhou, X.-H.4    Xu, M.-Y.5    Xu, W.-C.6
  • 181
    • 84978900742 scopus 로고    scopus 로고
    • Glutaminolysis as a target for cancer therapy
    • Jin, L., Alesi, G.N., and Kang, S. (2016) Glutaminolysis as a target for cancer therapy. Oncogene. 35, 3619-3625
    • (2016) Oncogene , vol.35 , pp. 3619-3625
    • Jin, L.1    Alesi, G.N.2    Kang, S.3
  • 182
    • 84927626428 scopus 로고    scopus 로고
    • CtBP maintains cancer cell growth and metabolic homeostasis via regulating SIRT4
    • Wang, L., Zhou, H., Wang, Y., Cui, G., and Di, L.-J. (2015) CtBP maintains cancer cell growth and metabolic homeostasis via regulating SIRT4. Cell Death Dis. 6, e1620
    • (2015) Cell Death Dis. , vol.6 , pp. e1620
    • Wang, L.1    Zhou, H.2    Wang, Y.3    Cui, G.4    Di, L.-J.5
  • 183
    • 84964000479 scopus 로고    scopus 로고
    • Clinical and therapeutic significance of sirtuin-4 expression in colorectal cancer
    • Huang, G., Cheng, J., Yu, F., Liu, X., Yuan, C., Liu, C., Chen, X., and Peng, Z. (2016) Clinical and therapeutic significance of sirtuin-4 expression in colorectal cancer. Oncol. Rep. 35, 2801-2810
    • (2016) Oncol. Rep. , vol.35 , pp. 2801-2810
    • Huang, G.1    Cheng, J.2    Yu, F.3    Liu, X.4    Yuan, C.5    Liu, C.6    Chen, X.7    Peng, Z.8
  • 184
    • 84930519237 scopus 로고    scopus 로고
    • Sirtuin-4 (SIRT4) is downregulated and associated with some clinicopathological features in gastric adenocarcinoma
    • Huang, G., Cui, F., Yu, F., Lu, H., Zhang, M., Tang, H., and Peng, Z. (2015) Sirtuin-4 (SIRT4) is downregulated and associated with some clinicopathological features in gastric adenocarcinoma. Biomed. Pharmacother. 72, 135-139
    • (2015) Biomed. Pharmacother. , vol.72 , pp. 135-139
    • Huang, G.1    Cui, F.2    Yu, F.3    Lu, H.4    Zhang, M.5    Tang, H.6    Peng, Z.7
  • 185
    • 84958191269 scopus 로고    scopus 로고
    • Loss of mitochondrial tumor suppressor genes expression is associated with unfavorable clinical outcome in head and neck squamous cell carcinoma: Data from retrospective study
    • Mahjabeen, I., and Kayani, M. A. (2016) Loss of mitochondrial tumor suppressor genes expression is associated with unfavorable clinical outcome in head and neck squamous cell carcinoma: data from retrospective study. PLoS One 11, e0146948
    • (2016) PLoS One , vol.11 , pp. e0146948
    • Mahjabeen, I.1    Kayani, M.A.2
  • 188
    • 84894109588 scopus 로고    scopus 로고
    • SIRT4 protein suppresses tumor formationin genetic models of Myc-induced Bcell lymphoma
    • Jeong, S.M., Lee, A., Lee, J., and Haigis, M. C. (2014) SIRT4 protein suppresses tumor formationin genetic models of Myc-induced Bcell lymphoma. J. Biol. Chem. 289, 4135-4144
    • (2014) J. Biol. Chem. , vol.289 , pp. 4135-4144
    • Jeong, S.M.1    Lee, A.2    Lee, J.3    Haigis, M.C.4
  • 191
    • 84944742172 scopus 로고    scopus 로고
    • Aging and chronic administration of serotonin-selective reuptake inhibitor citalopram upregulate Sirt4 gene expression in the preoptic area of malemice
    • Wong, D. W., Soga, T., and Parhar, I. S. (2015) Aging and chronic administration of serotonin-selective reuptake inhibitor citalopram upregulate Sirt4 gene expression in the preoptic area of malemice. Front. Genet. 6, 281
    • (2015) Front. Genet. , vol.6 , pp. 281
    • Wong, D.W.1    Soga, T.2    Parhar, I.S.3
  • 192
    • 80052273758 scopus 로고    scopus 로고
    • Neuronal Glud1 (glutamatedehydrogenase 1) over-expressing mice: Increased glutamate formation and synaptic release, loss of synaptic activity, and adaptive changes in genomic expression
    • Michaelis, E. K., Wang, X., Pal, R., Bao, X., Hascup, K. N., Wang, Y., Wang, W.-T., Hui, D., Agbas, A., Choi, I.-Y., Belousov, A., and Gerhardt, G.A. (2011) Neuronal Glud1 (glutamatedehydrogenase 1) over-expressing mice: increased glutamate formation and synaptic release, loss of synaptic activity, and adaptive changes in genomic expression. Neurochem. Int. 59, 473-481
    • (2011) Neurochem. Int. , vol.59 , pp. 473-481
    • Michaelis, E.K.1    Wang, X.2    Pal, R.3    Bao, X.4    Hascup, K.N.5    Wang, Y.6    Wang, W.-T.7    Hui, D.8    Agbas, A.9    Choi, I.-Y.10    Belousov, A.11    Gerhardt, G.A.12
  • 193
    • 84896257334 scopus 로고    scopus 로고
    • High altitude exposure alters gene expression levels of DNA repair enzymes, and modulates fatty acid metabolism by SIRT4 induction in human skeletal muscle
    • Acs, Z., Bori, Z., Takeda, M., Osvath, P., Berkes, I., Taylor, A.W., Yang, H., and Radak, Z. (2014) High altitude exposure alters gene expression levels of DNA repair enzymes, and modulates fatty acid metabolism by SIRT4 induction in human skeletal muscle. Respir. Physiol. Neurobiol. 196, 33-37
    • (2014) Respir. Physiol. Neurobiol. , vol.196 , pp. 33-37
    • Acs, Z.1    Bori, Z.2    Takeda, M.3    Osvath, P.4    Berkes, I.5    Taylor, A.W.6    Yang, H.7    Radak, Z.8
  • 194
    • 84942514336 scopus 로고    scopus 로고
    • Characterization of the cardiac succinylome and its role in ischemia-reperfusion injury
    • Boylston, J.A., Sun, J., Chen, Y., Gucek, M., Sack, M.N., and Murphy, E. (2015) Characterization of the cardiac succinylome and its role in ischemia-reperfusion injury. J. Mol. Cell. Cardiol. 88, 73-81
    • (2015) J. Mol. Cell. Cardiol. , vol.88 , pp. 73-81
    • Boylston, J.A.1    Sun, J.2    Chen, Y.3    Gucek, M.4    Sack, M.N.5    Murphy, E.6
  • 196
    • 37349110355 scopus 로고    scopus 로고
    • Metabolic adaptations through the PGC-1α and SIRT1 pathways
    • Rodgers, J.T., Lerin, C., Gerhart-Hines, Z., and Puigserver, P. (2008) Metabolic adaptations through the PGC-1α and SIRT1 pathways. FEBS Lett. 582, 46-53
    • (2008) FEBS Lett. , vol.582 , pp. 46-53
    • Rodgers, J.T.1    Lerin, C.2    Gerhart-Hines, Z.3    Puigserver, P.4
  • 198
    • 65249087389 scopus 로고    scopus 로고
    • SIRT5Deacetylates carbamoyl phosphate synthetase 1 and regulates the urea cycle
    • Nakagawa, T., Lomb, D. J., Haigis, M. C., and Guarente, L. (2009) SIRT5Deacetylates carbamoyl phosphate synthetase 1 and regulates the urea cycle. Cell 137, 560-570
    • (2009) Cell , vol.137 , pp. 560-570
    • Nakagawa, T.1    Lomb, D.J.2    Haigis, M.C.3    Guarente, L.4
  • 200
    • 56449117024 scopus 로고    scopus 로고
    • AMPK: A metabolic gauge regulating whole-body energy homeostasis
    • Lage, R., Diéguez, C., Vidal-Puig, A., and López, M. (2008) AMPK: a metabolic gauge regulating whole-body energy homeostasis. Trends Mol. Med. 14, 539-549
    • (2008) Trends Mol. Med. , vol.14 , pp. 539-549
    • Lage, R.1    Diéguez, C.2    Vidal-Puig, A.3    López, M.4
  • 201
    • 46049084164 scopus 로고    scopus 로고
    • Alcohol alters hepatic FoxO1, p53, and mitochondrial SIRT5 deacetylation function
    • Lieber, C. S., Leo, M.A., Wang, X., and Decarli, L.M. (2008) Alcohol alters hepatic FoxO1, p53, and mitochondrial SIRT5 deacetylation function. Biochem. Biophys. Res. Commun. 373, 246-252
    • (2008) Biochem. Biophys. Res. Commun. , vol.373 , pp. 246-252
    • Lieber, C.S.1    Leo, M.A.2    Wang, X.3    Decarli, L.M.4
  • 202
    • 84928587149 scopus 로고    scopus 로고
    • SIRT5 facilitates cancer cell growth and drug resistance in non-small cell lung cancer
    • Lu, W., Zuo, Y., Feng, Y., and Zhang, M. (2014) SIRT5 facilitates cancer cell growth and drug resistance in non-small cell lung cancer. Tumour Biol. 35, 10699-10705
    • (2014) Tumour Biol. , vol.35 , pp. 10699-10705
    • Lu, W.1    Zuo, Y.2    Feng, Y.3    Zhang, M.4
  • 204
    • 20444409132 scopus 로고    scopus 로고
    • Mouse Sir2 homolog SIRT6 is a nuclear ADP-ribosyltransferase
    • Liszt, G., Ford, E., Kurtev, M., and Guarente, L. (2005) Mouse Sir2 homolog SIRT6 is a nuclear ADP-ribosyltransferase. J. Biol. Chem. 280, 21313-21320
    • (2005) J. Biol. Chem. , vol.280 , pp. 21313-21320
    • Liszt, G.1    Ford, E.2    Kurtev, M.3    Guarente, L.4
  • 209
    • 84890569395 scopus 로고    scopus 로고
    • SIRT6, a protein withmany faces
    • Gertler, A. A., and Cohen, H. Y. (2013) SIRT6, a protein withmany faces. Biogerontology 14, 629-639
    • (2013) Biogerontology , vol.14 , pp. 629-639
    • Gertler, A.A.1    Cohen, H.Y.2
  • 210
    • 84892851452 scopus 로고    scopus 로고
    • Chromatin and beyond: The multitasking roles for SIRT6
    • Kugel, S., and Mostoslavsky, R. (2014) Chromatin and beyond: the multitasking roles for SIRT6. Trends Biochem. Sci. 39, 72-81
    • (2014) Trends Biochem. Sci. , vol.39 , pp. 72-81
    • Kugel, S.1    Mostoslavsky, R.2
  • 211
    • 84962026722 scopus 로고    scopus 로고
    • The complex role of SIRT6 in carcinogenesis
    • Lerrer, B., Gertler, A. A., and Cohen, H. Y. (2016) The complex role of SIRT6 in carcinogenesis. Carcinogenesis 37, 108-118
    • (2016) Carcinogenesis , vol.37 , pp. 108-118
    • Lerrer, B.1    Gertler, A.A.2    Cohen, H.Y.3
  • 215
    • 84865414333 scopus 로고    scopus 로고
    • Transcriptional integration of mitochondrial biogenesis
    • Scarpulla, R. C., Vega, R. B., and Kelly, D. P. (2012) Transcriptional integration of mitochondrial biogenesis. Trends Endocrinol. Metab. 23, 459-466
    • (2012) Trends Endocrinol. Metab. , vol.23 , pp. 459-466
    • Scarpulla, R.C.1    Vega, R.B.2    Kelly, D.P.3
  • 218
    • 84927130669 scopus 로고    scopus 로고
    • Cyclic AMP signaling reduces sirtuin 6 expression in non-small cell lung cancer cells by promoting ubiquitin-proteasomal degradation via inhibition of the Raf-MEKERK (Raf/mitogen-activated extracellular signal-regulated kinase/extracellular signal-regulated kinase) pathway
    • Kim, E.-J., and Juhnn, Y.-S. (2015) Cyclic AMP signaling reduces sirtuin 6 expression in non-small cell lung cancer cells by promoting ubiquitin-proteasomal degradation via inhibition of the Raf-MEKERK (Raf/mitogen-activated extracellular signal-regulated kinase/extracellular signal-regulated kinase) pathway. J. Biol. Chem. 290, 9604-9613
    • (2015) J. Biol. Chem. , vol.290 , pp. 9604-9613
    • Kim, E.-J.1    Juhnn, Y.-S.2
  • 219
    • 0035023128 scopus 로고    scopus 로고
    • Adipose tissue tumor necrosis factor and interleukin-6 expression in human obesity and insulin resistance
    • Kern, P. A., Ranganathan, S., Li, C., Wood, L., and Ranganathan, G. (2001) Adipose tissue tumor necrosis factor and interleukin-6 expression in human obesity and insulin resistance. Am. J. Physiol. Endocrinol. Metab. 280, E745-E751
    • (2001) Am. J. Physiol. Endocrinol. Metab. , vol.280 , pp. E745-E751
    • Kern, P.A.1    Ranganathan, S.2    Li, C.3    Wood, L.4    Ranganathan, G.5
  • 220
    • 79952032653 scopus 로고    scopus 로고
    • Activation of peroxisome proliferator-activated receptor gamma by rosiglitazone increases sirt6 expression and ameliorates hepatic steatosis in rats
    • Yang, S. J., Choi, J.M., Chae, S. W., Kim, W. J., Park, S. E., Rhee, E. J., Lee, W. Y., Oh, K.W., Park, S. W., Kim, S. W., and Park, C.-Y. (2011) Activation of peroxisome proliferator-activated receptor gamma by rosiglitazone increases sirt6 expression and ameliorates hepatic steatosis in rats. PLoS One 6, e17057
    • (2011) PLoS One , vol.6 , pp. e17057
    • Yang, S.J.1    Choi, J.M.2    Chae, S.W.3    Kim, W.J.4    Park, S.E.5    Rhee, E.J.6    Lee, W.Y.7    Oh, K.W.8    Park, S.W.9    Kim, S.W.10    Park, C.-Y.11
  • 221
    • 84870203841 scopus 로고    scopus 로고
    • Anti-inflammatory properties of sirtuin 6 in human umbilical vein endothelial cells
    • Lappas, M. (2012) Anti-inflammatory properties of sirtuin 6 in human umbilical vein endothelial cells. Mediators Inflamm. 2012, 597514
    • (2012) Mediators Inflamm. , vol.2012 , pp. 597514
    • Lappas, M.1
  • 224
    • 84880068090 scopus 로고    scopus 로고
    • The role of SIRT6 protein in agingand reprogramming of human induced pluripotentstem cells
    • Sharma, A., Diecke, S., Zhang, W. Y., Lan, F., He, C., Mordwinkin, N.M., Chua, K. F., and Wu, J.C. (2013) The role of SIRT6 protein in agingand reprogramming of human induced pluripotentstem cells. J. Biol. Chem. 288, 18439-18447
    • (2013) J. Biol. Chem. , vol.288 , pp. 18439-18447
    • Sharma, A.1    Diecke, S.2    Zhang, W.Y.3    Lan, F.4    He, C.5    Mordwinkin, N.M.6    Chua, K.F.7    Wu, J.C.8
  • 225
    • 84955337844 scopus 로고    scopus 로고
    • Reciprocal regulation between SIRT6 and miR-122 controls liver metabolism and predicts hepatocarcinoma prognosis
    • Elhanati, S., Ben-Hamo, R., Kanfi, Y., Varvak, A., Glazz, R., Lerrer, B., Efroni, S., and Cohen, H. Y. (2016) Reciprocal regulation between SIRT6 and miR-122 controls liver metabolism and predicts hepatocarcinoma prognosis. Cell Reports 14, 234-242
    • (2016) Cell Reports , vol.14 , pp. 234-242
    • Elhanati, S.1    Ben-Hamo, R.2    Kanfi, Y.3    Varvak, A.4    Glazz, R.5    Lerrer, B.6    Efroni, S.7    Cohen, H.Y.8
  • 229
    • 84888003905 scopus 로고    scopus 로고
    • Hsa-miR-125b suppresses bladder cancer development by down-regulating oncogene SIRT7 and oncogenic long noncoding RNA MALAT1
    • Han, Y., Liu, Y., Zhang, H., Wang, T., Diao, R., Jiang, Z., Gui, Y., and Cai, Z. (2013) Hsa-miR-125b suppresses bladder cancer development by down-regulating oncogene SIRT7 and oncogenic long noncoding RNA MALAT1. FEBS Lett. 587, 3875-3882
    • (2013) FEBS Lett. , vol.587 , pp. 3875-3882
    • Han, Y.1    Liu, Y.2    Zhang, H.3    Wang, T.4    Diao, R.5    Jiang, Z.6    Gui, Y.7    Cai, Z.8
  • 230
    • 84874487252 scopus 로고    scopus 로고
    • Sirtuin7 oncogenic potential in human hepatocellular carcinoma and its regulation by the tumor suppressors MiR-125a-5p and MiR-125b
    • Kim, J. K., Noh, J. H., Jung, K. H., Eun, J. W., Bae, H. J., Kim, M. G., Chang, Y. G., Shen, Q., Park, W. S., Lee, J. Y., Borlak, J., and Nam, S. W. (2013) Sirtuin7 oncogenic potential in human hepatocellular carcinoma and its regulation by the tumor suppressors MiR-125a-5p and MiR-125b. Hepatology 57, 1055-1067
    • (2013) Hepatology , vol.57 , pp. 1055-1067
    • Kim, J.K.1    Noh, J.H.2    Jung, K.H.3    Eun, J.W.4    Bae, H.J.5    Kim, M.G.6    Chang, Y.G.7    Shen, Q.8    Park, W.S.9    Lee, J.Y.10    Borlak, J.11    Nam, S.W.12
  • 231
    • 84951326022 scopus 로고    scopus 로고
    • C/EBPα negatively regulates SIRT7 expression via recruiting HDAC3 to the upstreampromoter of hepatocellular carcinoma cells
    • Liu, G. F., Lu, J. Y., Zhang, Y. J., Zhang, L. X., Lu, G. D., Xie, Z. J., Cheng, M. B., Shen, Y. F., and Zhang, Y. (2016) C/EBPα negatively regulates SIRT7 expression via recruiting HDAC3 to the upstreampromoter of hepatocellular carcinoma cells. Biochim. Biophys. Acta 1859, 348-354
    • (2016) Biochim. Biophys. Acta , vol.1859 , pp. 348-354
    • Liu, G.F.1    Lu, J.Y.2    Zhang, Y.J.3    Zhang, L.X.4    Lu, G.D.5    Xie, Z.J.6    Cheng, M.B.7    Shen, Y.F.8    Zhang, Y.9
  • 233
    • 62449117918 scopus 로고    scopus 로고
    • MiR-34, SIRT1 and p53: The feedback loop
    • Yamakuchi, M., and Lowenstein, C. J. (2009) MiR-34, SIRT1 and p53: the feedback loop. Cell Cycle 8, 712-715
    • (2009) Cell Cycle , vol.8 , pp. 712-715
    • Yamakuchi, M.1    Lowenstein, C.J.2
  • 234
    • 84910065689 scopus 로고    scopus 로고
    • MicroRNA-125b inhibits lens epithelial cell apoptosis by targeting p53 in age-related cataract
    • Qin, Y., Zhao, J., Min, X., Wang, M., Luo, W., Wu, D., Yan, Q., Li, J., Wu, X., and Zhang, J. (2014) MicroRNA-125b inhibits lens epithelial cell apoptosis by targeting p53 in age-related cataract. Biochim. Biophys. Acta 1842, 2439-2447
    • (2014) Biochim. Biophys. Acta , vol.1842 , pp. 2439-2447
    • Qin, Y.1    Zhao, J.2    Min, X.3    Wang, M.4    Luo, W.5    Wu, D.6    Yan, Q.7    Li, J.8    Wu, X.9    Zhang, J.10
  • 235
    • 0039728235 scopus 로고    scopus 로고
    • P53 Represses CAAT enhancer-binding protein (C/EBP)-dependent transcription of the albumin gene
    • Kubicka, S., Ku, F., Zender, L., Rudolph, K. L., Manns, M., and Trautwein, C. (1999) p53 Represses CAAT enhancer-binding protein (C/EBP)-dependent transcription of the albumin gene. J. Biol. Chem. 274, 32137-32144
    • (1999) J. Biol. Chem. , vol.274 , pp. 32137-32144
    • Kubicka, S.1    Ku, F.2    Zender, L.3    Rudolph, K.L.4    Manns, M.5    Trautwein, C.6
  • 236
    • 77949495196 scopus 로고    scopus 로고
    • The RNApolymerase I transcription machinery: An emerging target for the treatment of cancer
    • Drygin, D., Rice, W.G., and Grummt, I. (2010) The RNApolymerase I transcription machinery: an emerging target for the treatment of cancer. Annu. Rev. Pharmacol. Toxicol. 50, 131-156
    • (2010) Annu. Rev. Pharmacol. Toxicol. , vol.50 , pp. 131-156
    • Drygin, D.1    Rice, W.G.2    Grummt, I.3
  • 237
    • 64849107827 scopus 로고    scopus 로고
    • Involvement of SIRT7 in resumption of rDNA transcription at the exit from mitosis
    • Grob, A., Roussel, P., Wright, J. E., McStay, B., Hernandez-Verdun, D., and Sirri, V. (2009) Involvement of SIRT7 in resumption of rDNA transcription at the exit from mitosis. J. Cell Sci. 122, 489-498
    • (2009) J. Cell Sci. , vol.122 , pp. 489-498
    • Grob, A.1    Roussel, P.2    Wright, J.E.3    McStay, B.4    Hernandez-Verdun, D.5    Sirri, V.6
  • 238
    • 84925265469 scopus 로고    scopus 로고
    • A mitochondrial UPR-mediated metabolic checkpoint regulates hematopoietic stem cell aging
    • Mohrin, M., Shin, J., Liu, Y., Brown, K., and Luo, H. (2015) A mitochondrial UPR-mediated metabolic checkpoint regulates hematopoietic stem cell aging. Science 347, 1374-1377
    • (2015) Science , vol.347 , pp. 1374-1377
    • Mohrin, M.1    Shin, J.2    Liu, Y.3    Brown, K.4    Luo, H.5
  • 239
    • 41449083867 scopus 로고    scopus 로고
    • Sirt7 increases stress resistance of cardiomyocytes and prevents apoptosis and inflammatory cardiomyopathy in mice
    • Vakhrusheva, O., Smolka, C., Gajawada, P., Kostin, S., Boettger, T., Kubin, T., Braun, T., and Bober, E. (2008) Sirt7 increases stress resistance of cardiomyocytes and prevents apoptosis and inflammatory cardiomyopathy in mice. Circ. Res. 102, 703-710
    • (2008) Circ. Res. , vol.102 , pp. 703-710
    • Vakhrusheva, O.1    Smolka, C.2    Gajawada, P.3    Kostin, S.4    Boettger, T.5    Kubin, T.6    Braun, T.7    Bober, E.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.