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Volumn 38, Issue 5, 2012, Pages 349-359

Sirtuin activators and inhibitors

Author keywords

Resveratrol; Sirtuin activators; Sirtuin inhibitors; Sirtuins; SRT1720

Indexed keywords

1,4 DIHYDROPYRIDINE DERIVATIVE; AGK 2; CAMBINOL; CAMPTOTHECIN; CISPLATIN; ENZYME ACTIVATOR; ENZYME INHIBITOR; IMIDAZO[1,2 BETA]THIAZOLE DERIVATIVE; LONGEVINEX; NICOTINAMIDE; OXAZOLO[4,5 BETA]PYRIDINE DERIVATIVE; PLACEBO; PREDNISONE; RESVERATROL; RESVIDA; SALERMIDE; SIRTINOL; SIRTUIN; SIRTUIN ACTIVATOR; SIRTUIN INHIBITOR; SPLITOMICIN; SRT 1460; SRT 1720; SRT 2104; SRT 2183; SRT 2379; SURAMIN; TENOVIN; UNCLASSIFIED DRUG;

EID: 84867702707     PISSN: 09516433     EISSN: 18728081     Source Type: Journal    
DOI: 10.1002/biof.1032     Document Type: Review
Times cited : (305)

References (111)
  • 1
    • 0035826271 scopus 로고    scopus 로고
    • Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans
    • Tissenbaum H. A. and Guarente, L. (2001) Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans. Nature 410, 227-230.
    • (2001) Nature , vol.410 , pp. 227-230
    • Tissenbaum, H.A.1    Guarente, L.2
  • 2
    • 8644224064 scopus 로고    scopus 로고
    • Sir2 mediates longevity in the fly through a pathway related to calorie restriction
    • Rogina, B. and Helfand, S. L. (2004) Sir2 mediates longevity in the fly through a pathway related to calorie restriction. Proc. Natl. Acad. Sci. USA 101, 15998-16003.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 15998-16003
    • Rogina, B.1    Helfand, S.L.2
  • 3
    • 3142740860 scopus 로고    scopus 로고
    • Calorie restriction promotes mammalian cell survival by inducing the SIRT1 deacetylase
    • Cohen, H. Y., Miller, C., Bitterman, K. J., Wall, N. R., Hekking, B., et al. (2004) Calorie restriction promotes mammalian cell survival by inducing the SIRT1 deacetylase, Science 305, 390-392.
    • (2004) Science , vol.305 , pp. 390-392
    • Cohen, H.Y.1    Miller, C.2    Bitterman, K.J.3    Wall, N.R.4    Hekking, B.5
  • 4
    • 80053168829 scopus 로고    scopus 로고
    • Absence of effects of Sir2 overexpression on lifespan in C. elegans and Drosophila
    • Burnett, C., Valentini, S., Cabreiro, F., Goss, M., Somogyvári, M., et al. (2011) Absence of effects of Sir2 overexpression on lifespan in C. elegans and Drosophila, Nature, 477, 482-485.
    • (2011) Nature , vol.477 , pp. 482-485
    • Burnett, C.1    Valentini, S.2    Cabreiro, F.3    Goss, M.4    Somogyvári, M.5
  • 5
    • 0034705129 scopus 로고    scopus 로고
    • The silencing protein SIR2 and its homologs are NAD-dependent protein deacetylases
    • Landry, J., Sutton, A., Tafrov, S. T., Heller, R. C., Stebbins, J., et al. (2000) The silencing protein SIR2 and its homologs are NAD-dependent protein deacetylases. Proc. Natl. Acad. Sci. USA 97, 5807-5811.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 5807-5811
    • Landry, J.1    Sutton, A.2    Tafrov, S.T.3    Heller, R.C.4    Stebbins, J.5
  • 6
    • 35748957521 scopus 로고    scopus 로고
    • Recent advances in the medicinal chemistry of histone deacetylase inhibitors
    • Brittain, W. H. and Ottow, E. (2007) Recent advances in the medicinal chemistry of histone deacetylase inhibitors. Ann. Rep. Med. Chem. 42, 337-348.
    • (2007) Ann. Rep. Med. Chem. , vol.42 , pp. 337-348
    • Brittain, W.H.1    Ottow, E.2
  • 7
    • 34249083199 scopus 로고    scopus 로고
    • Sirtuins in mammals: insights into their biological function
    • Michan, S. and Sinclair, D. (2007) Sirtuins in mammals: insights into their biological function. Biochem. J. 404, 1-13.
    • (2007) Biochem. J. , vol.404 , pp. 1-13
    • Michan, S.1    Sinclair, D.2
  • 8
    • 0035913903 scopus 로고    scopus 로고
    • hSIR2 (SIRT1) functions as an NAD-dependent p53 deacetylase
    • Vaziri, H., Dessain, S. K., Ng Eaton, E., Imai, S. I., Frye, R. A., et al. (2001) hSIR2 (SIRT1) functions as an NAD-dependent p53 deacetylase. Cell 107, 149-159.
    • (2001) Cell , vol.107 , pp. 149-159
    • Vaziri, H.1    Dessain, S.K.2    Ng Eaton, E.3    Imai, S.I.4    Frye, R.A.5
  • 9
    • 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., 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
  • 10
    • 39149122568 scopus 로고    scopus 로고
    • Interphase nucleo-cytoplasmic shuttling and localization of SIRT2 during mitosis
    • North, B. J. and Verdin, E. (2007) Interphase nucleo-cytoplasmic shuttling and localization of SIRT2 during mitosis. PLoS One 2, e784.
    • (2007) PLoS One , vol.2
    • North, B.J.1    Verdin, E.2
  • 11
    • 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
  • 12
    • 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., et al. (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
  • 13
    • 39049184073 scopus 로고    scopus 로고
    • Chromosomal organization and fluorescence in situ hybridization of the human Sirtuin 6 gene
    • Mahlknecht, U., Ho, A. D., and Voelter-Mahlknecht, S. (2006) Chromosomal organization and fluorescence in situ hybridization of the human Sirtuin 6 gene, Int. J. Oncol. 28, 447-456.
    • (2006) Int. J. Oncol. , vol.28 , pp. 447-456
    • Mahlknecht, U.1    Ho, A.D.2    Voelter-Mahlknecht, S.3
  • 14
    • 77956462423 scopus 로고    scopus 로고
    • Role of Sirtuin 1 in metabolic regulation
    • Silva, J. P. and Wahlestedt, C. (2010) Role of Sirtuin 1 in metabolic regulation. Drug Discov. Today 15, 781-791.
    • (2010) Drug Discov. Today , vol.15 , pp. 781-791
    • Silva, J.P.1    Wahlestedt, C.2
  • 15
    • 18144411313 scopus 로고    scopus 로고
    • SIRT1 functionally interacts with the metabolic regulator and transcriptional coactivator PGC-1{alpha}
    • Nemoto, S., Fergusson, M. M., and Finkel, T. (2005) SIRT1 functionally interacts with the metabolic regulator and transcriptional coactivator PGC-1{alpha}. J. Biol. Chem. 280, 16456-16460.
    • (2005) J. Biol. Chem. , vol.280 , pp. 16456-16460
    • Nemoto, S.1    Fergusson, M.M.2    Finkel, T.3
  • 16
    • 14544282413 scopus 로고    scopus 로고
    • Nutrient control of glucose homeostasis through a complex of PGC-1alpha and SIRT1
    • Rodgers, J. T., Lerin, C., Haas, W., Gygi, S. P., Spiegelman, B. M., et al. (2005) Nutrient control of glucose homeostasis through a complex of PGC-1alpha and SIRT1. Nature 434, 113-118.
    • (2005) Nature , vol.434 , pp. 113-118
    • Rodgers, J.T.1    Lerin, C.2    Haas, W.3    Gygi, S.P.4    Spiegelman, B.M.5
  • 17
    • 54049158932 scopus 로고    scopus 로고
    • Brain SIRT1: anatomical distribution and regulation by energy availability
    • Ramadori, G., Lee, C. E., Bookout, A. L., Lee, S., Williams, K. W., et al. (2008) Brain SIRT1: anatomical distribution and regulation by energy availability. J. Neurosci. 28, 9989-9996.
    • (2008) J. Neurosci. , vol.28 , pp. 9989-9996
    • Ramadori, G.1    Lee, C.E.2    Bookout, A.L.3    Lee, S.4    Williams, K.W.5
  • 18
    • 77956644726 scopus 로고    scopus 로고
    • SIRT1 deacetylase in POMC neurons is required for homeostatic defenses against diet-induced obesity
    • Ramadori, G., Fujikawa, T., Fukuda, M., Anderson, J., Morgan, D. A., et al. (2010) SIRT1 deacetylase in POMC neurons is required for homeostatic defenses against diet-induced obesity. Cell Metab. 12, 78-87.
    • (2010) Cell Metab. , vol.12 , pp. 78-87
    • Ramadori, G.1    Fujikawa, T.2    Fukuda, M.3    Anderson, J.4    Morgan, D.A.5
  • 19
    • 84655167647 scopus 로고    scopus 로고
    • Association of sirtuin 1 (SIRT1) gene SNPs and transcript expression levels with severe obesity
    • Clark, S. J., Falchi, M., Olsson, B., Jacobson, P., Cauchi, S., et al. (2012) Association of sirtuin 1 (SIRT1) gene SNPs and transcript expression levels with severe obesity. Obesity (Silver Spring) 20, 178-185.
    • (2012) Obesity (Silver Spring) , vol.20 , pp. 178-185
    • Clark, S.J.1    Falchi, M.2    Olsson, B.3    Jacobson, P.4    Cauchi, S.5
  • 20
    • 29744463503 scopus 로고    scopus 로고
    • Sirtuin 1 (SIRT1) sequence variation is not associated with exceptional human longevity
    • Flachsbart, F., Croucher, P. J., Nikolaus, S., Hampe, J., Cordes, C., et al. (2006) Sirtuin 1 (SIRT1) sequence variation is not associated with exceptional human longevity. Exp. Gerontol. 41, 98-102.
    • (2006) Exp. Gerontol. , vol.41 , pp. 98-102
    • Flachsbart, F.1    Croucher, P.J.2    Nikolaus, S.3    Hampe, J.4    Cordes, C.5
  • 21
    • 67650563916 scopus 로고    scopus 로고
    • SirT1 is an inhibitor of proliferation and tumor formation in colon cancer
    • Kabra, N., Li, Z., Chen, L., Li, B., Zhang, X., et al. (2009) SirT1 is an inhibitor of proliferation and tumor formation in colon cancer. J. Biol. Chem. 284, 18210-18217.
    • (2009) J. Biol. Chem. , vol.284 , pp. 18210-18217
    • Kabra, N.1    Li, Z.2    Chen, L.3    Li, B.4    Zhang, X.5
  • 23
    • 79959866409 scopus 로고    scopus 로고
    • Nicotinamide blocks proliferation and induces apoptosis of chronic lymphocytic leukemia cells through activation of the p53/miR-34a/SIRT1 tumor suppressor network
    • Audrito, V., Vaisitti, T., Rossi, D., Gottardi, D., D'Arena, G., et al. (2011) Nicotinamide blocks proliferation and induces apoptosis of chronic lymphocytic leukemia cells through activation of the p53/miR-34a/SIRT1 tumor suppressor network. Cancer Res. 71, 4473-4483.
    • (2011) Cancer Res. , vol.71 , pp. 4473-4483
    • Audrito, V.1    Vaisitti, T.2    Rossi, D.3    Gottardi, D.4    D'Arena, G.5
  • 24
    • 53149137486 scopus 로고    scopus 로고
    • Impaired DNA damage response, genome instability, and tumorigenesis in SIRT1 mutant mice
    • Wang, R. H., Sengupta, K., Li, C., Kim, H. S., Cao, L., et al. (2008) Impaired DNA damage response, genome instability, and tumorigenesis in SIRT1 mutant mice. Cancer Cell. 14, 312-323.
    • (2008) Cancer Cell. , vol.14 , pp. 312-323
    • Wang, R.H.1    Sengupta, K.2    Li, C.3    Kim, H.S.4    Cao, L.5
  • 25
    • 33847793039 scopus 로고    scopus 로고
    • Sirtuin 2, a mammalian 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., et al. (2007) Sirtuin 2, a mammalian 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
  • 26
    • 0037405043 scopus 로고    scopus 로고
    • Role for human SIRT2 NAD-dependent deacetylase activity in control of mitotic exit in the cell cycle
    • Dryden, S. C., Nahhas, F. A., Nowak, J. E., Goustin, A. S., and Tainsky, M. A. (2003) Role for human SIRT2 NAD-dependent deacetylase activity in control of mitotic exit in the cell cycle. Mol. Cell. Biol. 23, 3173-3185.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 3173-3185
    • Dryden, S.C.1    Nahhas, F.A.2    Nowak, J.E.3    Goustin, A.S.4    Tainsky, M.A.5
  • 27
    • 0041829415 scopus 로고    scopus 로고
    • Proteomics-based identification of differentially expressed genes in human gliomas: down-regulation of SIRT2 gene
    • Hiratsuka, M., Inoue, T., Toda, T., Kimura, N., Shirayoshi, Y., et al. (2003) Proteomics-based identification of differentially expressed genes in human gliomas: down-regulation of SIRT2 gene. Biochem. Biophys. Res. Commun. 309, 558-566.
    • (2003) Biochem. Biophys. Res. Commun. , vol.309 , pp. 558-566
    • Hiratsuka, M.1    Inoue, T.2    Toda, T.3    Kimura, N.4    Shirayoshi, Y.5
  • 28
    • 80054769188 scopus 로고    scopus 로고
    • SIRT2 maintains genome integrity and suppresses tumorigenesis through regulating APC/C activity
    • Kim, H. S., Vassilopoulos, A., Wang, R. H., Lahusen, T., Xiao, Z., et al. (2011) SIRT2 maintains genome integrity and suppresses tumorigenesis through regulating APC/C activity. Cancer Cell 20, 487-499.
    • (2011) Cancer Cell , vol.20 , pp. 487-499
    • Kim, H.S.1    Vassilopoulos, A.2    Wang, R.H.3    Lahusen, T.4    Xiao, Z.5
  • 29
    • 78649328799 scopus 로고    scopus 로고
    • Sirtuin regulation of mitochondria: energy production, apoptosis, and signaling
    • Verdin, E., Hirschey, M. D., Finley, L. W., and Haigis, M. C. (2010) Sirtuin regulation of mitochondria: energy production, apoptosis, and signaling. Trends Biochem. Sci. 35, 669-675.
    • (2010) Trends Biochem. Sci. , vol.35 , pp. 669-675
    • Verdin, E.1    Hirschey, M.D.2    Finley, L.W.3    Haigis, M.C.4
  • 30
    • 19944433088 scopus 로고    scopus 로고
    • A novel VNTR enhancer within the SIRT3 gene, a human homologue of SIR2, is associated with survival at oldest ages
    • Bellizzi, D., Rose, G., Cavalcante, P., Covello, G., Dato, S., et al. (2005) A novel VNTR enhancer within the SIRT3 gene, a human homologue of SIR2, is associated with survival at oldest ages. Genomics 85, 258-263.
    • (2005) Genomics , vol.85 , pp. 258-263
    • Bellizzi, D.1    Rose, G.2    Cavalcante, P.3    Covello, G.4    Dato, S.5
  • 31
    • 79958041304 scopus 로고    scopus 로고
    • Fine tuning our cellular factories: sirtuins in mitochondrial biology
    • Zhong, L. and Mostoslavsky, R. (2011) Fine tuning our cellular factories: sirtuins in mitochondrial biology. Cell Metab. 13, 621-626.
    • (2011) Cell Metab. , vol.13 , pp. 621-626
    • Zhong, L.1    Mostoslavsky, R.2
  • 32
    • 77953285831 scopus 로고    scopus 로고
    • Function and regulation of the mitochondrial sirtuin isoform Sirt5 in Mammalia
    • Gertz, M. and Steegborn, C. (2010) Function and regulation of the mitochondrial sirtuin isoform Sirt5 in Mammalia. Biochim. Biophys. Acta. 1804, 1658-1665.
    • (2010) Biochim. Biophys. Acta. , vol.1804 , pp. 1658-1665
    • Gertz, M.1    Steegborn, C.2
  • 33
    • 79959363092 scopus 로고    scopus 로고
    • SIRT6 promotes DNA repair under stress by activating PARP1
    • Mao, Z., Hine, C., Tian, X., Van Meter, M., Au, M., et al. (2011) SIRT6 promotes DNA repair under stress by activating PARP1. Science 332, 1443-1446.
    • (2011) Science , vol.332 , pp. 1443-1446
    • Mao, Z.1    Hine, C.2    Tian, X.3    Van Meter, M.4    Au, M.5
  • 34
    • 31044445366 scopus 로고    scopus 로고
    • Genomic instability and aging-like phenotype in the absence of mammalian SIRT6
    • Mostoslavsky, R., Chua, K. F., Lombard, D. B., Pang, W. W., Fischer, M. R., et al. (2006) Genomic instability and aging-like phenotype in the absence of mammalian SIRT6. Cell 124, 315-329.
    • (2006) Cell , vol.124 , pp. 315-329
    • Mostoslavsky, R.1    Chua, K.F.2    Lombard, D.B.3    Pang, W.W.4    Fischer, M.R.5
  • 35
    • 80052908853 scopus 로고    scopus 로고
    • SIRT6 overexpression induces massive apoptosis in cancer cells but not in normal cells
    • Van Meter, M., Mao, Z., Gorbunova, V., and Seluanov, A. (2011) SIRT6 overexpression induces massive apoptosis in cancer cells but not in normal cells. Cell Cycle 10, 3153-3158.
    • (2011) Cell Cycle , vol.10 , pp. 3153-3158
    • Van Meter, M.1    Mao, Z.2    Gorbunova, V.3    Seluanov, A.4
  • 36
    • 64049090625 scopus 로고    scopus 로고
    • Sirt7-dependent inhibition of cell growth and proliferation might be instrumental to mediate tissue integrity during aging
    • Vakhrusheva, O., Braeuer, D., Liu, Z., Braun, T., and Bober, E. (2008) Sirt7-dependent inhibition of cell growth and proliferation might be instrumental to mediate tissue integrity during aging. J. Physiol. Pharmacol. 59, 201-212.
    • (2008) J. Physiol. Pharmacol. , vol.59 , pp. 201-212
    • Vakhrusheva, O.1    Braeuer, D.2    Liu, Z.3    Braun, T.4    Bober, E.5
  • 37
    • 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., et al. (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
  • 38
    • 84861140340 scopus 로고    scopus 로고
    • Functional proteomics establishes the interaction of SIRT7 with chromatin remodeling complexes and expands its role in regulation of RNA polymerase I transcription
    • Tsai, Y. C., Greco, T. M., Boonmee, A., Miteva, Y., and Cristea, I. M. (2012) Functional proteomics establishes the interaction of SIRT7 with chromatin remodeling complexes and expands its role in regulation of RNA polymerase I transcription. Mol. Cell. Proteomics 11, M111 015156.
    • (2012) Mol. Cell. Proteomics , vol.11
    • Tsai, Y.C.1    Greco, T.M.2    Boonmee, A.3    Miteva, Y.4    Cristea, I.M.5
  • 40
    • 0034703217 scopus 로고    scopus 로고
    • Requirement of NAD and SIR2 for life-span extension by calorie restriction in Saccharomyces cerevisiae
    • Lin, S. J., Defossez, P. A., and Guarente, L. (2000) Requirement of NAD and SIR2 for life-span extension by calorie restriction in Saccharomyces cerevisiae. Science 289, 2126-2128.
    • (2000) Science , vol.289 , pp. 2126-2128
    • Lin, S.J.1    Defossez, P.A.2    Guarente, L.3
  • 41
    • 0141719702 scopus 로고    scopus 로고
    • Small molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan
    • Howitz, K. T., Bitterman, K. J., Cohen, H. Y., Lamming, D. W., Lavu, S., et al. (2003) Small molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan. Nature 425, 191-196.
    • (2003) Nature , vol.425 , pp. 191-196
    • Howitz, K.T.1    Bitterman, K.J.2    Cohen, H.Y.3    Lamming, D.W.4    Lavu, S.5
  • 42
    • 3943071801 scopus 로고    scopus 로고
    • Sirtuin activators mimic caloric restriction and delay ageing in metazoans
    • Helfand, S. L.
    • Wood, J. G., Rogina, B., Lavu, S., Howitz, K., and Helfand, S. L. (2004) Sirtuin activators mimic caloric restriction and delay ageing in metazoans. Nature 430, 686-689.
    • (2004) Nature , vol.430 , pp. 686-689
    • Wood, J.G.1    Rogina, B.2    Lavu, S.3    Howitz, K.4
  • 43
    • 49649128314 scopus 로고    scopus 로고
    • Short-term consumption of a resveratrol-containing nutraceutical mixture mimics gene expression of long-term caloric restriction in mouse heart
    • Barger, J. L., Kayo, T., Pugh, T. D., Prolla, T. A., and Weindruch, R. (2008) Short-term consumption of a resveratrol-containing nutraceutical mixture mimics gene expression of long-term caloric restriction in mouse heart. Exp. Gerontol. 43, 859-866.
    • (2008) Exp. Gerontol. , vol.43 , pp. 859-866
    • Barger, J.L.1    Kayo, T.2    Pugh, T.D.3    Prolla, T.A.4    Weindruch, R.5
  • 44
    • 48349144852 scopus 로고    scopus 로고
    • Resveratrol delays age-related deterioration and mimics transcriptional aspects of dietary restriction without extending life span
    • Pearson, K. J., Baur, J. A., Lewis, K. N., Peshkin, L., Price, N. L., et al. (2008) Resveratrol delays age-related deterioration and mimics transcriptional aspects of dietary restriction without extending life span. Cell Metab. 8, 157-168.
    • (2008) Cell Metab. , vol.8 , pp. 157-168
    • Pearson, K.J.1    Baur, J.A.2    Lewis, K.N.3    Peshkin, L.4    Price, N.L.5
  • 45
    • 33746824192 scopus 로고    scopus 로고
    • Neuronal SIRT1 activation as a novel mechanism underlying the prevention of Alzheimer disease amyloid neuropathology by calorie restriction
    • Qin, W., Yang, T., Ho, L., Zhao, Z., Wang, J., et al. (2006) Neuronal SIRT1 activation as a novel mechanism underlying the prevention of Alzheimer disease amyloid neuropathology by calorie restriction. J. Biol. Chem. 281, 21745-21754.
    • (2006) J. Biol. Chem. , vol.281 , pp. 21745-21754
    • Qin, W.1    Yang, T.2    Ho, L.3    Zhao, Z.4    Wang, J.5
  • 46
    • 34447308268 scopus 로고    scopus 로고
    • SIRT1 deacetylase protects against neurodegeneration in models for Alzheimer's disease and amyotrophic lateral sclerosis
    • Kim, D., Nguyen, M. D., Dobbin, M. M., Fischer, A., Sananbenesi, F., et al. (2007) SIRT1 deacetylase protects against neurodegeneration in models for Alzheimer's disease and amyotrophic lateral sclerosis, EMBO J. 26, 3169-3179.
    • (2007) EMBO J. , vol.26 , pp. 3169-3179
    • Kim, D.1    Nguyen, M.D.2    Dobbin, M.M.3    Fischer, A.4    Sananbenesi, F.5
  • 48
    • 79959261445 scopus 로고    scopus 로고
    • What is new for an old molecule? Systematic review and recommendations on the use of resveratrol
    • Vang, O., Ahmad, N., Baile, C. A., Baur, J. A., Brown, K., et al. (2011) What is new for an old molecule? Systematic review and recommendations on the use of resveratrol. PLoS One 6, e19881.
    • (2011) PLoS One , vol.6
    • Vang, O.1    Ahmad, N.2    Baile, C.A.3    Baur, J.A.4    Brown, K.5
  • 49
    • 33751072349 scopus 로고    scopus 로고
    • Resveratrol improves health and survival of mice on a high-calorie diet
    • Baur, J. A., Pearson, K. J., Price, N. L., Jamieson, H. A., Lerin, C., et al. (2006) Resveratrol improves health and survival of mice on a high-calorie diet. Nature 444, 337-342.
    • (2006) Nature , vol.444 , pp. 337-342
    • Baur, J.A.1    Pearson, K.J.2    Price, N.L.3    Jamieson, H.A.4    Lerin, C.5
  • 50
    • 80455143206 scopus 로고    scopus 로고
    • Calorie restriction-like effects of 30 days of resveratrol supplementation on energy metabolism and metabolic profile in obese humans
    • Timmers, S., Konings, E., Bilet, L., Houtkooper, R. H., van de Weijer, T., et al. (2011) Calorie restriction-like effects of 30 days of resveratrol supplementation on energy metabolism and metabolic profile in obese humans. Cell Metab. 14, 612-622.
    • (2011) Cell Metab. , vol.14 , pp. 612-622
    • Timmers, S.1    Konings, E.2    Bilet, L.3    Houtkooper, R.H.4    van de Weijer, T.5
  • 51
    • 84950170835 scopus 로고    scopus 로고
    • Acute resveratrol supplementation improves flow-mediated dilatation in overweight/obese individuals with mildly elevated blood pressure
    • Wong, R. H., Howe, P. R., Buckley, J. D., Coates, A. M., Kunz, I., et al. (2011) Acute resveratrol supplementation improves flow-mediated dilatation in overweight/obese individuals with mildly elevated blood pressure. Nutr. Metab. Cardiovasc. Dis. 21, 851-856.
    • (2011) Nutr. Metab. Cardiovasc. Dis. , vol.21 , pp. 851-856
    • Wong, R.H.1    Howe, P.R.2    Buckley, J.D.3    Coates, A.M.4    Kunz, I.5
  • 52
    • 82455220960 scopus 로고    scopus 로고
    • Modified resveratrol Longevinex improves endothelial function in adults with metabolic syndrome receiving standard treatment
    • Fujitaka, K., Otani, H., Jo, F., Jo, H., Nomura, E., et al. (2011) Modified resveratrol Longevinex improves endothelial function in adults with metabolic syndrome receiving standard treatment. Nutr. Res. 31, 842-847.
    • (2011) Nutr. Res. , vol.31 , pp. 842-847
    • Fujitaka, K.1    Otani, H.2    Jo, F.3    Jo, H.4    Nomura, E.5
  • 53
    • 63549094179 scopus 로고    scopus 로고
    • Small molecule activators of SIRT1 replicate signaling pathways triggered by calorie restriction in vivo
    • Smith, J. J., Kenney, R. D., Gagne, D. J., Frushour, B. P., Ladd, W., et al. (2009) Small molecule activators of SIRT1 replicate signaling pathways triggered by calorie restriction in vivo. BMC Syst. Biol. 3, 31.
    • (2009) BMC Syst. Biol. , vol.3 , pp. 31
    • Smith, J.J.1    Kenney, R.D.2    Gagne, D.J.3    Frushour, B.P.4    Ladd, W.5
  • 54
    • 80052572943 scopus 로고    scopus 로고
    • Phase I randomized, double-blind pilot study of micronized resveratrol (SRT501) in patients with hepatic metastases-safety, pharmacokinetics, and pharmacodynamics
    • Howells, L. M., Berry, D. P., Elliott, P. J., Jacobson, E. W., Hoffmann, E., et al. (2011) Phase I randomized, double-blind pilot study of micronized resveratrol (SRT501) in patients with hepatic metastases-safety, pharmacokinetics, and pharmacodynamics. Cancer Prev. Res. (Phila) 4, 1419-1425.
    • (2011) Cancer Prev. Res. (Phila) , vol.4 , pp. 1419-1425
    • Howells, L.M.1    Berry, D.P.2    Elliott, P.J.3    Jacobson, E.W.4    Hoffmann, E.5
  • 55
    • 36749087548 scopus 로고    scopus 로고
    • Small molecule activators of SIRT1 as therapeutics for the treatment of type 2 diabetes
    • Milne, J. C., Lambert, P. D., Schenk, S., Carney, D. P., Smith, J. J., et al. (2007) Small molecule activators of SIRT1 as therapeutics for the treatment of type 2 diabetes. Nature 450, 712-716.
    • (2007) Nature , vol.450 , pp. 712-716
    • Milne, J.C.1    Lambert, P.D.2    Schenk, S.3    Carney, D.P.4    Smith, J.J.5
  • 56
    • 54849425547 scopus 로고    scopus 로고
    • Specific SIRT1 activation mimics low energy levels and protects against diet-induced metabolic disorders by enhancing fat oxidation
    • Feige, J. N., Lagouge, M., Canto, C., Strehle, A., Houten, S. M., et al. (2008) Specific SIRT1 activation mimics low energy levels and protects against diet-induced metabolic disorders by enhancing fat oxidation. Cell Metab. 8, 347-358.
    • (2008) Cell Metab. , vol.8 , pp. 347-358
    • Feige, J.N.1    Lagouge, M.2    Canto, C.3    Strehle, A.4    Houten, S.M.5
  • 57
    • 77951049870 scopus 로고    scopus 로고
    • SRT1720 induces mitochondrial biogenesis and rescues mitochondrial function after oxidant injury in renal proximal tubule cells
    • Funk, J. A., Odejinmi, S., and Schnellmann, R. G. (2010) SRT1720 induces mitochondrial biogenesis and rescues mitochondrial function after oxidant injury in renal proximal tubule cells. J. Pharmacol. Exp. Ther. 333, 593-601.
    • (2010) J. Pharmacol. Exp. Ther. , vol.333 , pp. 593-601
    • Funk, J.A.1    Odejinmi, S.2    Schnellmann, R.G.3
  • 58
    • 70350452395 scopus 로고    scopus 로고
    • Treatment with SRT1720, a SIRT1 activator, ameliorates fatty liver with reduced expression of lipogenic enzymes in MSG mice
    • Yamazaki, Y., Usui, I., Kanatani, Y., Matsuya, Y., Tsuneyama, K., et al. (2009) Treatment with SRT1720, a SIRT1 activator, ameliorates fatty liver with reduced expression of lipogenic enzymes in MSG mice. Am. J. Physiol. Endocrinol. Metab. 297, E 1179-1186.
    • (2009) Am. J. Physiol. Endocrinol. Metab. , vol.297
    • Yamazaki, Y.1    Usui, I.2    Kanatani, Y.3    Matsuya, Y.4    Tsuneyama, K.5
  • 59
    • 84859909860 scopus 로고    scopus 로고
    • SRT1720 suppresses apoptosis and restores a more normal gene expression profile indicative of reduced inflammation in the livers of mice fed a high-fat diet. Scientific Reports 1, 10.1038/srep00070.
    • Minor, R. K., Baur, J. A., Gomes, A. P., Ward, T. M., Csiszar, A., et al. (2011) SRT1720 suppresses apoptosis and restores a more normal gene expression profile indicative of reduced inflammation in the livers of mice fed a high-fat diet. Scientific Reports 1, 10.1038/srep00070.
    • (2011)
    • Minor, R.K.1    Baur, J.A.2    Gomes, A.P.3    Ward, T.M.4    Csiszar, A.5
  • 60
    • 81155148158 scopus 로고    scopus 로고
    • Preclinical evaluation of a novel SIRT1 modulator SRT1720 in multiple myeloma cells
    • Chauhan, D., Bandi, M., Singh, A. V., Ray, A., Raje, N., et al. (2011) Preclinical evaluation of a novel SIRT1 modulator SRT1720 in multiple myeloma cells. Br. J. Haematol. 155, 588-598.
    • (2011) Br. J. Haematol. , vol.155 , pp. 588-598
    • Chauhan, D.1    Bandi, M.2    Singh, A.V.3    Ray, A.4    Raje, N.5
  • 61
    • 63149150180 scopus 로고    scopus 로고
    • Discovery of oxazolo[4,5-b]pyridines and related heterocyclic analogs as novel SIRT1 activators
    • Bemis, J. E., Vu, C. B., Xie, R., Nunes, J. J., Ng, P. Y., et al. (2009) Discovery of oxazolo[4, 5-b]pyridines and related heterocyclic analogs as novel SIRT1 activators. Bioorg. Med. Chem. Lett. 19, 2350-2353.
    • (2009) Bioorg. Med. Chem. Lett. , vol.19 , pp. 2350-2353
    • Bemis, J.E.1    Vu, C.B.2    Xie, R.3    Nunes, J.J.4    Ng, P.Y.5
  • 62
    • 64349118889 scopus 로고    scopus 로고
    • Discovery of imidazo[1,2-b]thiazole derivatives as novel SIRT1 activators
    • Vu, C. B., Bemis, J. E., Disch, J. S., Ng, P. Y., Nunes, J. J., et al. (2009) Discovery of imidazo[1, 2-b]thiazole derivatives as novel SIRT1 activators. J. Med. Chem. 52, 1275-1283.
    • (2009) J. Med. Chem. , vol.52 , pp. 1275-1283
    • Vu, C.B.1    Bemis, J.E.2    Disch, J.S.3    Ng, P.Y.4    Nunes, J.J.5
  • 63
    • 84867737204 scopus 로고    scopus 로고
    • SRT2104, a novel and selective small molecule SIRT1 activator, inhibits DSS-induced colitis in a SIRT1-dependent manner, 10th World Congress on Inflammation, Paris.
    • Ellis, D. J. G. J. L., Suri, V., Cermak, J. M., Lyng, G. D., Guarente, L. P., and Vlasuk, G. P. (2011) SRT2104, a novel and selective small molecule SIRT1 activator, inhibits DSS-induced colitis in a SIRT1-dependent manner, 10th World Congress on Inflammation, Paris.
    • (2011)
    • Ellis, D.J.G.J.L.1    Suri, V.2    Cermak, J.M.3    Lyng, G.D.4    Guarente, L.P.5    Vlasuk, G.P.6
  • 64
    • 84876203344 scopus 로고    scopus 로고
    • The first demonstration of clinical activity by a small molecule sirt1 activator: srt2104 reduces cytokine release and coagulation activation in a human endotoxemia model., 10th World Congress on Inflammation, Paris.
    • Van Der Meer, A., Scicluna, B., Lin, J., Jacobson, E., Vlasuk, G. P., et al. (2011) The first demonstration of clinical activity by a small molecule sirt1 activator: srt2104 reduces cytokine release and coagulation activation in a human endotoxemia model., 10th World Congress on Inflammation, Paris.
    • (2011)
    • Van Der Meer, A.1    Scicluna, B.2    Lin, J.3    Jacobson, E.4    Vlasuk, G.P.5
  • 65
    • 33751560439 scopus 로고    scopus 로고
    • SIRT1 modulating compounds from high-throughput screening as anti-inflammatory and insulin-sensitizing agents
    • Nayagam, V. M., Wang, X., Tan, Y. C., Poulsen, A., Goh, K. C., et al. (2006) SIRT1 modulating compounds from high-throughput screening as anti-inflammatory and insulin-sensitizing agents. J. Biomol. Screen. 11, 959-967.
    • (2006) J. Biomol. Screen. , vol.11 , pp. 959-967
    • Nayagam, V.M.1    Wang, X.2    Tan, Y.C.3    Poulsen, A.4    Goh, K.C.5
  • 66
    • 69949096844 scopus 로고    scopus 로고
    • Study of 1,4-dihydropyridine structural scaffold: discovery of novel sirtuin activators and inhibitors
    • Mai, A., Valente, S., Meade, S., Carafa, V., Tardugno, M., et al. (2009) Study of 1, 4-dihydropyridine structural scaffold: discovery of novel sirtuin activators and inhibitors. J. Med. Chem. 52, 5496-5504.
    • (2009) J. Med. Chem. , vol.52 , pp. 5496-5504
    • Mai, A.1    Valente, S.2    Meade, S.3    Carafa, V.4    Tardugno, M.5
  • 67
    • 70350524083 scopus 로고    scopus 로고
    • Resveratrol is not a direct activator of SIRT1 enzyme activity
    • Beher, D., Wu, J., Cumine, S., Kim, K. W., Lu, S. C., et al. (2009) Resveratrol is not a direct activator of SIRT1 enzyme activity. Chem. Biol. Drug Des. 74, 619-624.
    • (2009) Chem. Biol. Drug Des. , vol.74 , pp. 619-624
    • Beher, D.1    Wu, J.2    Cumine, S.3    Kim, K.W.4    Lu, S.C.5
  • 68
    • 20444444649 scopus 로고    scopus 로고
    • Mechanism of human SIRT1 activation by resveratrol
    • Borra, M. T., Smith, B. C., and Denu, J. M. (2005) Mechanism of human SIRT1 activation by resveratrol. J. Biol. Chem. 280, 17187-17195.
    • (2005) J. Biol. Chem. , vol.280 , pp. 17187-17195
    • Borra, M.T.1    Smith, B.C.2    Denu, J.M.3
  • 69
    • 78650184332 scopus 로고    scopus 로고
    • SIRT1-independent mechanisms of the putative sirtuin enzyme activators SRT1720 and SRT2183
    • Huber, J. L., Mcburney, M. W., Distefano, P. S., and Mcdonagh, T. (2010) SIRT1-independent mechanisms of the putative sirtuin enzyme activators SRT1720 and SRT2183. Future Med. Chem. 2, 1751-1759.
    • (2010) Future Med. Chem. , vol.2 , pp. 1751-1759
    • Huber, J.L.1    Mcburney, M.W.2    Distefano, P.S.3    and Mcdonagh, T.4
  • 71
    • 77950246109 scopus 로고    scopus 로고
    • SRT1720, SRT2183, SRT1460, and resveratrol are not direct activators of SIRT1
    • Pacholec, M., Bleasdale, J. E., Chrunyk, B., Cunningham, D., Flynn, D., et al. (2010) SRT1720, SRT2183, SRT1460, and resveratrol are not direct activators of SIRT1. J. Biol. Chem. 285, 8340-8351.
    • (2010) J. Biol. Chem. , vol.285 , pp. 8340-8351
    • Pacholec, M.1    Bleasdale, J.E.2    Chrunyk, B.3    Cunningham, D.4    Flynn, D.5
  • 72
    • 40849135481 scopus 로고    scopus 로고
    • The Sirtuin family: therapeutic targets to treat diseases of aging
    • Milne, J. C. and Denu, J. M. (2008) The Sirtuin family: therapeutic targets to treat diseases of aging. Curr. Opin. Chem. Biol. 12, 11-17.
    • (2008) Curr. Opin. Chem. Biol. , vol.12 , pp. 11-17
    • Milne, J.C.1    Denu, J.M.2
  • 73
    • 9444296057 scopus 로고    scopus 로고
    • High absorption but very low bioavailability of oral resveratrol in humans
    • Walle, U. K.
    • Walle, T., Hsieh, F., Delegge, M. H., Oatis, J. E., Jr, and Walle, U. K. (2004) High absorption but very low bioavailability of oral resveratrol in humans. Drug Metab. Dispos. 32, 1377-1382.
    • (2004) Drug Metab. Dispos. , vol.32 , pp. 1377-1382
    • Walle, T.1    Hsieh, F.2    Delegge, M.H.3    Oatis Jr, J.E.4
  • 74
    • 77958488312 scopus 로고    scopus 로고
    • SIRT1 activation by small molecules: kinetic and biophysical evidence for direct interaction of enzyme and activator
    • Dai, H., Kustigian, L., Carney, D., Case, A., Considine, T., et al. (2010) SIRT1 activation by small molecules: kinetic and biophysical evidence for direct interaction of enzyme and activator. J. Biol. Chem. 285, 32695-32703.
    • (2010) J. Biol. Chem. , vol.285 , pp. 32695-32703
    • Dai, H.1    Kustigian, L.2    Carney, D.3    Case, A.4    Considine, T.5
  • 75
    • 67349276169 scopus 로고    scopus 로고
    • AMPK regulates energy expenditure by modulating NAD+ metabolism and SIRT1 activity
    • Canto, C., Gerhart-Hines, Z., Feige, J. N., Lagouge, M., Noriega, L., et al. (2009) AMPK regulates energy expenditure by modulating NAD+ metabolism and SIRT1 activity. Nature 458, 1056-1060.
    • (2009) Nature , vol.458 , pp. 1056-1060
    • Canto, C.1    Gerhart-Hines, Z.2    Feige, J.N.3    Lagouge, M.4    Noriega, L.5
  • 76
    • 77249156847 scopus 로고    scopus 로고
    • Interdependence of AMPK and SIRT1 for metabolic adaptation to fasting and exercise in skeletal muscle
    • Canto, C., Jiang, L. Q., Deshmukh, A. S., Mataki, C., Coste, A., et al. (2010) Interdependence of AMPK and SIRT1 for metabolic adaptation to fasting and exercise in skeletal muscle. Cell Metab. 11, 213-219.
    • (2010) Cell Metab. , vol.11 , pp. 213-219
    • Canto, C.1    Jiang, L.Q.2    Deshmukh, A.S.3    Mataki, C.4    Coste, A.5
  • 77
    • 84863011114 scopus 로고    scopus 로고
    • Resveratrol ameliorates aging-related metabolic phenotypes by inhibiting cAMP phosphodiesterases
    • Park, S. J., Ahmad, F., Philp, A., Baar, K., Williams, T., et al. (2012) Resveratrol ameliorates aging-related metabolic phenotypes by inhibiting cAMP phosphodiesterases. Cell 148, 421-433.
    • (2012) Cell , vol.148 , pp. 421-433
    • Park, S.J.1    Ahmad, F.2    Philp, A.3    Baar, K.4    Williams, T.5
  • 78
    • 0041571570 scopus 로고    scopus 로고
    • Sir2 regulation by nicotinamide results from switching between base exchange and deacetylation chemistry
    • Sauve, A. A. and Schramm, V. L. (2003) Sir2 regulation by nicotinamide results from switching between base exchange and deacetylation chemistry. Biochemistry 42, 9249-9256.
    • (2003) Biochemistry , vol.42 , pp. 9249-9256
    • Sauve, A.A.1    Schramm, V.L.2
  • 79
    • 70349810821 scopus 로고    scopus 로고
    • Mechanistic studies on the effects of nicotinamide on megakaryocytic polyploidization and the roles of NAD+ levels and SIRT inhibition
    • e1343.
    • Giammona, L. M., Panuganti, S., Kemper, J. M., Apostolidis, P. A., Lindsey, S., et al. (2009) Mechanistic studies on the effects of nicotinamide on megakaryocytic polyploidization and the roles of NAD+ levels and SIRT inhibition. Exp. Hematol. 37, 1340-1352 e1343.
    • (2009) Exp. Hematol. , vol.37 , pp. 1340-1352
    • Giammona, L.M.1    Panuganti, S.2    Kemper, J.M.3    Apostolidis, P.A.4    Lindsey, S.5
  • 80
    • 34547599329 scopus 로고    scopus 로고
    • Sirtuin 2 inhibitors rescue alpha-synuclein-mediated toxicity in models of Parkinson's disease
    • Outeiro, T. F., Kontopoulos, E., Altmann, S. M., Kufareva, I., Strathearn, K. E., et al. (2007) Sirtuin 2 inhibitors rescue alpha-synuclein-mediated toxicity in models of Parkinson's disease. Science 317, 516-519.
    • (2007) Science , vol.317 , pp. 516-519
    • Outeiro, T.F.1    Kontopoulos, E.2    Altmann, S.M.3    Kufareva, I.4    Strathearn, K.E.5
  • 81
    • 18844362632 scopus 로고    scopus 로고
    • Stage-specific antileishmanial activity of an inhibitor of SIR2 histone deacetylase
    • Vergnes, B., Vanhille, L., Ouaissi, A., and Sereno, D. (2005) Stage-specific antileishmanial activity of an inhibitor of SIR2 histone deacetylase. Acta Trop. 94, 107-115.
    • (2005) Acta Trop. , vol.94 , pp. 107-115
    • Vergnes, B.1    Vanhille, L.2    Ouaissi, A.3    Sereno, D.4
  • 84
    • 79957968813 scopus 로고    scopus 로고
    • Medicinal chemistry of sirtuin inhibitors
    • Chen, L. (2011) Medicinal chemistry of sirtuin inhibitors. Curr. Med. Chem. 18, 1936-1946.
    • (2011) Curr. Med. Chem. , vol.18 , pp. 1936-1946
    • Chen, L.1
  • 87
    • 41649103241 scopus 로고    scopus 로고
    • Structure-activity studies on splitomicin derivatives as sirtuin inhibitors and computational prediction of binding mode
    • Neugebauer, R. C., Uchiechowska, U., Meier, R., Hruby, H., Valkov, V., et al. (2008) Structure-activity studies on splitomicin derivatives as sirtuin inhibitors and computational prediction of binding mode. J. Med. Chem. 51, 1203-1213.
    • (2008) J. Med. Chem. , vol.51 , pp. 1203-1213
    • Neugebauer, R.C.1    Uchiechowska, U.2    Meier, R.3    Hruby, H.4    Valkov, V.5
  • 88
    • 41949125454 scopus 로고    scopus 로고
    • SIRT1 inhibition alleviates gene silencing in Fragile X mental retardation syndrome
    • Biacsi, R., Kumari, D., and Usdin, K. (2008) SIRT1 inhibition alleviates gene silencing in Fragile X mental retardation syndrome. PLoS Genet. 4, e1000017.
    • (2008) PLoS Genet. , vol.4
    • Biacsi, R.1    Kumari, D.2    Usdin, K.3
  • 89
    • 0035914304 scopus 로고    scopus 로고
    • Identification of a class of small molecule inhibitors of the sirtuin family of NAD-dependent deacetylases by phenotypic screening
    • Grozinger, C. M., Chao, E. D., Blackwell, H. E., Moazed, D., and Schreiber, S. L. (2001) Identification of a class of small molecule inhibitors of the sirtuin family of NAD-dependent deacetylases by phenotypic screening. J. Biol. Chem. 276, 38837-38843.
    • (2001) J. Biol. Chem. , vol.276 , pp. 38837-38843
    • Grozinger, C.M.1    Chao, E.D.2    Blackwell, H.E.3    Moazed, D.4    Schreiber, S.L.5
  • 90
    • 28144438533 scopus 로고    scopus 로고
    • Design, synthesis, and biological evaluation of sirtinol analogues as class III histone/protein deacetylase (Sirtuin) inhibitors
    • Mai, A., Massa, S., Lavu, S., Pezzi, R., Simeoni, S., et al. (2005) Design, synthesis, and biological evaluation of sirtinol analogues as class III histone/protein deacetylase (Sirtuin) inhibitors. J. Med. Chem. 48, 7789-7795.
    • (2005) J. Med. Chem. , vol.48 , pp. 7789-7795
    • Mai, A.1    Massa, S.2    Lavu, S.3    Pezzi, R.4    Simeoni, S.5
  • 91
    • 30544445468 scopus 로고    scopus 로고
    • Sirt1 inhibitor, Sirtinol, induces senescence-like growth arrest with attenuated Ras-MAPK signaling in human cancer cells
    • Ota, H., Tokunaga, E., Chang, K., Hikasa, M., Iijima, K., et al. (2006) Sirt1 inhibitor, Sirtinol, induces senescence-like growth arrest with attenuated Ras-MAPK signaling in human cancer cells. Oncogene 25, 176-185.
    • (2006) Oncogene , vol.25 , pp. 176-185
    • Ota, H.1    Tokunaga, E.2    Chang, K.3    Hikasa, M.4    Iijima, K.5
  • 92
    • 79952398625 scopus 로고    scopus 로고
    • The effect of combined treatment with cisplatin and histone deacetylase inhibitors on HeLa cells
    • Jin, K. L., Park, J. Y., Noh, E. J., Hoe, K. L., Lee, J. H., et al. (2010) The effect of combined treatment with cisplatin and histone deacetylase inhibitors on HeLa cells. J. Gynecol. Oncol. 21, 262-268.
    • (2010) J. Gynecol. Oncol. , vol.21 , pp. 262-268
    • Jin, K.L.1    Park, J.Y.2    Noh, E.J.3    Hoe, K.L.4    Lee, J.H.5
  • 93
    • 47249154705 scopus 로고    scopus 로고
    • A role for SIRT1 in cell growth and chemoresistance in prostate cancer PC3 and DU145 cells
    • Kojima, K., Ohhashi, R., Fujita, Y., Hamada, N., Akao, Y., et al. (2008) A role for SIRT1 in cell growth and chemoresistance in prostate cancer PC3 and DU145 cells. Biochem. Biophys. Res. Commun. 373, 423-428.
    • (2008) Biochem. Biophys. Res. Commun. , vol.373 , pp. 423-428
    • Kojima, K.1    Ohhashi, R.2    Fujita, Y.3    Hamada, N.4    Akao, Y.5
  • 94
    • 77950835404 scopus 로고    scopus 로고
    • SIRT inhibitors induce cell death and p53 acetylation through targeting both SIRT1 and SIRT2
    • Peck, B., Chen, C. Y., Ho, K. K., Di Fruscia, P., Myatt, S. S., et al. (2010) SIRT inhibitors induce cell death and p53 acetylation through targeting both SIRT1 and SIRT2. Mol. Cancer Ther. 9, 844-855.
    • (2010) Mol. Cancer Ther. , vol.9 , pp. 844-855
    • Peck, B.1    Chen, C.Y.2    Ho, K.K.3    Di Fruscia, P.4    Myatt, S.S.5
  • 95
    • 79953799195 scopus 로고    scopus 로고
    • Sirtuin-3 (SIRT3), a novel potential therapeutic target for oral cancer
    • Alhazzazi, T. Y., Kamarajan, P., Joo, N., Huang, J. Y., Verdin, E., et al. (2011) Sirtuin-3 (SIRT3), a novel potential therapeutic target for oral cancer. Cancer 117, 1670-1678.
    • (2011) Cancer , vol.117 , pp. 1670-1678
    • Alhazzazi, T.Y.1    Kamarajan, P.2    Joo, N.3    Huang, J.Y.4    Verdin, E.5
  • 96
    • 46249124837 scopus 로고    scopus 로고
    • Sirtuin inhibition protects from the polyalanine muscular dystrophy protein PABPN1
    • Catoire, H., Pasco, M. Y., Abu-Baker, A., Holbert, S., Tourette, C., et al. (2008) Sirtuin inhibition protects from the polyalanine muscular dystrophy protein PABPN1. Hum. Mol. Genet. 17, 2108-2117.
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 2108-2117
    • Catoire, H.1    Pasco, M.Y.2    Abu-Baker, A.3    Holbert, S.4    Tourette, C.5
  • 97
    • 77249153712 scopus 로고    scopus 로고
    • Characterization of sirtuin inhibitors in nematodes expressing a muscular dystrophy protein reveals muscle cell and behavioral protection by specific sirtinol analogues
    • Pasco, M. Y., Rotili, D., Altucci, L., Farina, F., Rouleau, G. A., et al. (2010) Characterization of sirtuin inhibitors in nematodes expressing a muscular dystrophy protein reveals muscle cell and behavioral protection by specific sirtinol analogues. J. Med. Chem. 53, 1407-1411.
    • (2010) J. Med. Chem. , vol.53 , pp. 1407-1411
    • Pasco, M.Y.1    Rotili, D.2    Altucci, L.3    Farina, F.4    Rouleau, G.A.5
  • 98
    • 80052638751 scopus 로고    scopus 로고
    • Sirtinol treatment reduces inflammation in human dermal microvascular endothelial cells
    • Orecchia, A., Scarponi, C., Di Felice, F., Cesarini, E., Avitabile, S., et al. (2011) Sirtinol treatment reduces inflammation in human dermal microvascular endothelial cells. PLoS One 6, e24307.
    • (2011) PLoS One , vol.6
    • Orecchia, A.1    Scarponi, C.2    Di Felice, F.3    Cesarini, E.4    Avitabile, S.5
  • 99
    • 84855769254 scopus 로고    scopus 로고
    • SIRT2 activity is required for the survival of C6 glioma cells
    • He, X., Nie, H., Hong, Y., Sheng, C., Xia, W., et al. (2012) SIRT2 activity is required for the survival of C6 glioma cells. Biochem. Biophys. Res. Commun. 417, 468-472.
    • (2012) Biochem. Biophys. Res. Commun. , vol.417 , pp. 468-472
    • He, X.1    Nie, H.2    Hong, Y.3    Sheng, C.4    Xia, W.5
  • 100
    • 79954527563 scopus 로고    scopus 로고
    • Silencing of SIRT2 induces cell death and a decrease in the intracellular ATP level of PC12 cells
    • Nie, H., Chen, H., Han, J., Hong, Y., Ma, Y., et al. (2011) Silencing of SIRT2 induces cell death and a decrease in the intracellular ATP level of PC12 cells. Int. J. Physiol. Pathophysiol. Pharmacol. 3, 65-70.
    • (2011) Int. J. Physiol. Pathophysiol. Pharmacol. , vol.3 , pp. 65-70
    • Nie, H.1    Chen, H.2    Han, J.3    Hong, Y.4    Ma, Y.5
  • 102
    • 33646254136 scopus 로고    scopus 로고
    • Antitumor activity of a small-molecule inhibitor of human silent information regulator 2 enzymes
    • Heltweg, B., Gatbonton, T., Schuler, A. D., Posakony, J., Li, H., et al. (2006) Antitumor activity of a small-molecule inhibitor of human silent information regulator 2 enzymes. Cancer Res. 66, 4368-4377.
    • (2006) Cancer Res. , vol.66 , pp. 4368-4377
    • Heltweg, B.1    Gatbonton, T.2    Schuler, A.D.3    Posakony, J.4    Li, H.5
  • 103
    • 65649111534 scopus 로고    scopus 로고
    • Novel cambinol analogs as sirtuin inhibitors: synthesis, biological evaluation, and rationalization of activity
    • Medda, F., Russell, R. J., Higgins, M., Mccarthy, A. R., Campbell, J., et al. (2009) Novel cambinol analogs as sirtuin inhibitors: synthesis, biological evaluation, and rationalization of activity. J. Med. Chem. 52, 2673-2682.
    • (2009) J. Med. Chem. , vol.52 , pp. 2673-2682
    • Medda, F.1    Russell, R.J.2    Higgins, M.3    Mccarthy, A.R.4    Campbell, J.5
  • 104
    • 33847635635 scopus 로고    scopus 로고
    • Structural basis of inhibition of the human NAD+-dependent deacetylase SIRT5 by suramin
    • Schuetz, A., Min, J., Antoshenko, T., Wang, C. L., Allali-Hassani, A., et al. (2007) Structural basis of inhibition of the human NAD+-dependent deacetylase SIRT5 by suramin. Structure 15, 377-389.
    • (2007) Structure , vol.15 , pp. 377-389
    • Schuetz, A.1    Min, J.2    Antoshenko, T.3    Wang, C.L.4    Allali-Hassani, A.5
  • 105
    • 35548936745 scopus 로고    scopus 로고
    • Structure-activity studies on suramin analogues as inhibitors of NAD+-dependent histone deacetylases (sirtuins)
    • Trapp, J., Meier, R., Hongwiset, D., Kassack, M. U., Sippl, W., et al. (2007) Structure-activity studies on suramin analogues as inhibitors of NAD+-dependent histone deacetylases (sirtuins). ChemMedChem 2, 1419-1431.
    • (2007) ChemMedChem , vol.2 , pp. 1419-1431
    • Trapp, J.1    Meier, R.2    Hongwiset, D.3    Kassack, M.U.4    Sippl, W.5
  • 106
    • 18244409076 scopus 로고    scopus 로고
    • New agents in intravesical chemotherapy of superficial bladder cancer
    • Perabo, F. G. and Muller, S. C. (2005) New agents in intravesical chemotherapy of superficial bladder cancer. Scand. J. Urol. Nephrol. 39, 108-116.
    • (2005) Scand. J. Urol. Nephrol. , vol.39 , pp. 108-116
    • Perabo, F.G.1    Muller, S.C.2
  • 107
    • 42949114938 scopus 로고    scopus 로고
    • Discovery, in vivo activity, and mechanism of action of a small-molecule p53 activator
    • Lain, S., Hollick, J. J., Campbell, J., Staples, O. D., Higgins, M., et al. (2008) Discovery, in vivo activity, and mechanism of action of a small-molecule p53 activator. Cancer Cell 13, 454-463.
    • (2008) Cancer Cell , vol.13 , pp. 454-463
    • Lain, S.1    Hollick, J.J.2    Campbell, J.3    Staples, O.D.4    Higgins, M.5
  • 108
    • 84863116364 scopus 로고    scopus 로고
    • Activation of stress response gene SIRT1 by BCR-ABL promotes leukemogenesis
    • Yuan, H., Wang, Z., Li, L., Zhang, H., Modi, H., et al. (2012) Activation of stress response gene SIRT1 by BCR-ABL promotes leukemogenesis. Blood 119, 1904-1914.
    • (2012) Blood , vol.119 , pp. 1904-1914
    • Yuan, H.1    Wang, Z.2    Li, L.3    Zhang, H.4    Modi, H.5
  • 109
    • 84857355902 scopus 로고    scopus 로고
    • Synthesis and biological characterisation of sirtuin inhibitors based on the tenovins
    • McCarthy, A. R., Pirrie, L., Hollick, J. J., Ronseaux, S., Campbell, J., et al. (2012) Synthesis and biological characterisation of sirtuin inhibitors based on the tenovins. Bioorg. Med. Chem. 20, 1779-1793.
    • (2012) Bioorg. Med. Chem. , vol.20 , pp. 1779-1793
    • McCarthy, A.R.1    Pirrie, L.2    Hollick, J.J.3    Ronseaux, S.4    Campbell, J.5
  • 110
    • 60149091562 scopus 로고    scopus 로고
    • Salermide, a Sirtuin inhibitor with a strong cancer-specific proapoptotic effect
    • Lara, E., Mai, A., Calvanese, V., Altucci, L., Lopez-Nieva, P., et al. (2009) Salermide, a Sirtuin inhibitor with a strong cancer-specific proapoptotic effect. Oncogene 28, 781-791.
    • (2009) Oncogene , vol.28 , pp. 781-791
    • Lara, E.1    Mai, A.2    Calvanese, V.3    Altucci, L.4    Lopez-Nieva, P.5
  • 111
    • 84863103122 scopus 로고    scopus 로고
    • Salermide upregulates death receptor 5 expression through the ATF4-ATF3-CHOP axis and leads to apoptosis in human cancer cells
    • doi: 10.1111/j.1582-4934.2011.01401.x
    • Liu, G., Su, L., Hao, X., Zhong, N., Zhong, D., et al. (2011) Salermide upregulates death receptor 5 expression through the ATF4-ATF3-CHOP axis and leads to apoptosis in human cancer cells. J. Cell. Mol. Med. doi: 10.1111/j.1582-4934.2011.01401.x
    • (2011) J. Cell. Mol. Med.
    • Liu, G.1    Su, L.2    Hao, X.3    Zhong, N.4    Zhong, D.5


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