1 |
Uciechowska, U., Schemies, J., Neugebauer, R. C., Huda, E. M., Schmitt, M. L., Meier, R., Verdin, E., Jung, M. and Sippl, W. 2008. Thiobarbiturates as SIRT inhibitors: virtual screening, free-energy calculations, and biological testing. Chem. Med. Chem. 3, 1965-1976.
DOI
|
2 |
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.
DOI
|
3 |
Villalba, J. M. and Alcain, F. J. 2012. SIRT activators and inhibitors. Biofactors 38, 349-359.
DOI
|
4 |
Wang, C., Gao, F., Wu, J., Dai, J., Wei, C. and Li, Y. 2010. Arabidopsis putative deacetylase AtSRT2 regulates basal defense by suppressing PAD4, EDS5 and SID2 expression. Plant Cell Physiol. 51, 1291-1299.
DOI
|
5 |
Wang, J., Kim, T. H., Ahn, M. Y., Lee, J., Jung, J. H., Choi, W. S., Lee, B. M., Yoon, K. S., Yoon, S. and Kim, H. S. 2012. Sirtinol, a class III HDAC inhibitor, induces apoptotic and autophagic cell death in MCF-7 human breast cancer cells. Int. J. Oncol. 41, 1101-1109.
DOI
|
6 |
Xu, F., Zhang, Q., Zhang, K., Xie, W. and Grunstein, M. 2007. Sir2 deacetylates histone H3 lysine 56 to regulate telomeric heterochromatin structure in yeast. Mol. Cell. 27, 890-900.
DOI
|
7 |
Taylor, D. M., Balabadra, U., Xiang, Z., Woodman, B., Meade, S., Amore, A., Maxwell, M. M., Reeves, S., Bates, G. P., Luthi-Carter, R., Lowden, P. A. and Kazantsev, A. G. 2011. A brain-permeable small molecule reduces neuronal cholesterol by inhibiting activity of SIRT 2 deacetylase. ACS Chem. Biol. 6, 540-546.
DOI
|
8 |
Yamamoto, H., Schoonjans, K. and Auwerx, J. 2007. SIRT functions in health and disease. Mol. Endocrinol. 21, 1745-1755.
DOI
|
9 |
Yuan, H., Wang, Z., Li, L., Zhang, H., Modi, H., Horne, D., Bhatia, R. and Chen, W. 2012. Activation of stress response gene SIRT1 by BCR-ABL promotes leukemogenesis. Blood 119, 1904-1914.
DOI
|
10 |
Zeng, W., Dai, X., Sun, J., Hou, Y., Ma, X., Cao, X., Zhao, Y. and Cheng, Y. 2019. Modulation of auxin signaling and development by polyadenylation machinery. Plant Physiol. 179, 686-699.
DOI
|
11 |
Zhang, H., Lu, Y., Zhao, Y. and Zhou, D. X. 2016. OsSRT1 is involved in rice seed development through regulation of starch metabolism gene expression. Plant Sci. 248, 28-36.
DOI
|
12 |
Zhao, L., Lu, J., Zhang, J., Wu, P. Y., Yang, S. and Wu, K. 2014. Identification and characterization of histone deacetylases in tomato (Solanum lycopersicum). Front Plant Sci. 5, 760.
DOI
|
13 |
Zhao, Y., Dai, X., Blackwell, H. E., Schreiber, S. L. and Chory, J. 2003. SIR1, an upstream component in auxin signaling identified by chemical genetics. Science 301, 1107-1110.
DOI
|
14 |
Zhong, X., Zhang, H., Zhao, Y., Sun, Q., Hu, Y., Peng, H. and Zhou, D. X. 2013. The rice NAD(+)-dependent histone deacetylase OsSRT1 targets preferentially to stress- and metabolism-related genes and transposable elements. PLoS One 8, e66807.
DOI
|
15 |
Kaschani, F. and van der Hoorn, R. 2007. Small molecule approaches in plants. Curr. Opin. Chem. Biol. 11, 88-98.
DOI
|
16 |
Kojima, K., Ohhashi, R., Fujita, Y., Hamada, N., Akao, Y., Nozawa, Y., Deguchi, T. and Ito, M. 2008. A role for SIRT1 in cell growth and chemoresistance in prostate cancer PC3 and DU145 cells. Biochem. Biophys. Res. Commun. 373, 423-428.
DOI
|
17 |
Konig, A. C., Hartl, M., Pham, P. A., Laxa, M., Boersema, P. J., Orwat, A., Kalitventseva, I., Plochinger, M., Braun, H. P., Leister, D., Mann, M., Wachter, A., Fernie, A. R. and Finkemeier, I. 2014. The Arabidopsis class II SIRT is a lysine deacetylase and interacts with mitochondrial energy metabolism. Plant Physiol. 164, 1401-1414.
DOI
|
18 |
Kupis, W., Palyga, J., Tomal, E. and Niewiadomska, E. 2016. The role of SIRTs in cellular homeostasis. J. Physiol. Biochem. 72, 371-380.
DOI
|
19 |
Landry, J., Sutton, A., Tafrov, S. T., Heller, R. C., Stebbins, J., Pillus, L. and Sternglanz, R. 2000. The silencing protein SIR2 and its homologs are NAD-dependent protein deacetylases. Proc. Natl. Acad. Sci. USA. 97, 5807-5811.
DOI
|
20 |
Langsfeld, E. S., Bodily, J. M. and Laimins, L. A. 2015. The deacetylase SIRT 1 regulates human papillomavirus replication by modulating histone acetylation and recruitment of DNA damage factors NBS1 and Rad51 to viral genomes. PLoS Pathog. 11, e1005181.
DOI
|
21 |
Lara, E., Mai, A., Calvanese, V., Altucci, L., Lopez-Nieva, P., Martinez-Chantar, M. L., Varela-Rey, M., Rotili, D., Nebbioso, A., Ropero, S., Montoya, G., Oyarzabal, J., Velasco, S., Serrano, M., Witt, M., Villar-Garea, A., Imhof, A., Mato, J. M., Esteller, M. and Fraga, M. F. 2009. Salermide, a SIRT inhibitor with a strong cancer-specific proapoptotic effect. Oncogene 28, 781-791.
DOI
|
22 |
Lerrer, B., Gertler, A. A. and Cohen, H. Y. 2016. The complex role of SIRT6 in carcinogenesis. Carcinogenesis 37, 108-118.
DOI
|
23 |
Libro, R., Giacoppo, S., Soundara Rajan, T., Bramanti, P. and Mazzon, E. 2016. Natural phytochemicals in the treatment and prevention of dementia: an overview. Molecules 21, 518.
DOI
|
24 |
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.
DOI
|
25 |
Liu, P. Y., Xu, N., Malyukova, A., Scarlett, C. J., Sun, Y. T., Zhang, X. D., Ling, D., Su, S. P., Nelson, C., Chang, D. K., Koach, J., Tee, A. E., Haber, M., Norris, M. D., Toon, C., Rooman, I., Xue, C., Cheung, B. B., Kumar, S., Marshall, G. M., Biankin, A. V. and Liu, T. 2013. The histone deacetylase SIRT2 stabilizes Myc oncoproteins. Cell Death Differ. 20, 503-514.
DOI
|
26 |
Liu, X., Wei, W., Zhu, W., Su, L., Xiong, Z., Zhou, M., Zheng, Y. and Zhou, D. X. 2017. Histone deacetylase AtSRT1 links metabolic flux and stress response in arabidopsis. Mol. Plant 10, 1510-1522.
DOI
|
27 |
Luthi-Carter, R., Taylor, D. M., Pallos, J., Lambert, E., Amore, A., Parker, A., Moffitt, H., Smith, D. L., Runne, H., Gokce, O., Kuhn, A., Xiang, Z., Maxwell, M. M., Reeves, S. A., Bates, G. P., Neri, C., Thompson, L. M., Marsh, J. L. and Kazantsev, A. G. 2010. SIRT2 inhibition achieves neuroprotection by decreasing sterol biosynthesis. Proc. Natl. Acad. Sci. USA. 107, 7927-7932.
DOI
|
28 |
Marmorstein, R. 2001. Structure of histone deacetylases: insights into substrate recognition and catalysis. Structure 9, 1127-1133.
DOI
|
29 |
Mellini, P., Kokkola, T., Suuronen, T., Salo, H. S., Tolvanen, L., Mai, A., Lahtela-Kakkonen, M. and Jarho, E. M. 2013. Screen of pseudopeptidic inhibitors of human SIRTs 1-3: two lead compounds with antiproliferative effects in cancer cells. J. Med. Chem. 56, 6681-6695.
DOI
|
30 |
Michan, S. and Sinclair, D. 2007. SIRTs in mammals: insights into their biological function. Biochem. J. 404, 1-13.
DOI
|
31 |
Aquea, F., Timmermann, T. and Arce-Johnson, P. 2010. Analysis of histone acetyltransferase and deacetylase families of Vitis vinifera. Plant Physiol. Biochem. 48, 194-199.
DOI
|
32 |
Napper, A. D., Hixon, J., McDonagh, T., Keavey, K., Pons, J. F., Barker, J., Yau, W. T., Amouzegh, P., Flegg, A., Hamelin, E., Thomas, R. J., Kates, M., Jones, S., Navia, M. A., Saunders, J. O., DiStefano, P. S. and Curtis, R. 2005. Discovery of indoles as potent and selective inhibitors of the deacetylase SIRT1. J. Med. Chem. 48, 8045-8054.
DOI
|
33 |
Neugebauer, R. C., Uchiechowska, U., Meier, R., Hruby, H., Valkov, V., Verdin, E., Sippl, W. and Jung, M. 2008. Structure-activity studies on splitomicin derivatives as SIRT inhibitors and computational prediction of binding mode. J. Med. Chem. 51, 1203-1213.
DOI
|
34 |
Nguyen, H. N., Kim, J. H., Jeong, C. Y., Hong, S. W. and Lee, H. 2013. Inhibition of histone deacetylation alters Arabidopsis root growth in response to auxin via PIN1 degradation. Plant Cell Rep. 32, 1625-1636.
DOI
|
35 |
North, B. J. and Verdin, E. 2004. SIRTs: Sir2-related NAD-dependent protein deacetylases. Genome Biol. 5, 224.
DOI
|
36 |
Ota, H., Tokunaga, E., Chang, K., Hikasa, M., Iijima, K., Eto, M., Kozaki, K., Akishita, M., Ouchi, Y. and Kaneki, M. 2006. Sirt1 inhibitor, Sirtinol, induces senescence-like growth arrest with attenuated Ras-MAPK signaling in human cancer cells. Oncogene 25, 176-185.
DOI
|
37 |
Outeiro, T. F., Kontopoulos, E., Altmann, S. M., Kufareva, I., Strathearn, K. E., Amore, A. M., Volk, C. B., Maxwell, M. M., Rochet, J. C., McLean, P. J., Young, A. B., Abagyan, R., Feany, M. B., Hyman, B. T. and Kazantsev, A. G. 2007. SIRT 2 inhibitors rescue alpha-synuclein-mediated toxicity in models of Parkinson's disease. Science 317, 516-519.
DOI
|
38 |
Pagans, S., Pedal, A., North, B. J., Kaehlcke, K., Marshall, B. L., Dorr, A., Hetzer-Egger, C., Henklein, P., Frye, R., McBurney, M. W., Hruby, H., Jung, M., Verdin, E. and Ott, M. 2005. SIRT1 regulates HIV transcription via Tat deacetylation. PLoS Biol. 3, e41.
DOI
|
39 |
Audrito, V., Vaisitti, T., Rossi, D., Gottardi, D., D'Arena, G., Laurenti, L., Gaidano, G., Malavasi, F. and Deaglio, S. 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.
DOI
|
40 |
Bedalov, A., Gatbonton, T., Irvine, W. P., Gottschling, D. E. and Simon, J. A. 2001. Identification of a small molecule inhibitor of Sir2p. Proc. Natl. Acad. Sci. USA. 98, 15113-15118.
DOI
|
41 |
Biacsi, R., Kumari, D. and Usdin, K. 2008. SIRT1 inhibition alleviates gene silencing in Fragile X mental retardation syndrome. PLoS Genet. 4, e1000017.
DOI
|
42 |
Braunstein, M., Rose, A. B., Holmes, S. G., Allis, C. D. and Broach, J. R. 1993. Transcriptional silencing in yeast is associated with reduced nucleosome acetylation. Genes Dev. 7, 592-604.
DOI
|
43 |
Carafa, V., Rotili, D., Forgione, M., Cuomo, F., Serretiello, E., Hailu, G. S., Jarho, E., Lahtela-Kakkonen, M., Mai, A. and Altucci, L. 2016. SIRT functions and modulation: from chemistry to the clinic. Clin. Epigenetics 8, 61.
DOI
|
44 |
Dai, X., Hayashi, K., Nozaki, H., Cheng, Y. and Zhao, Y. 2005. Genetic and chemical analyses of the action mechanisms of sirtinol in Arabidopsis. Proc. Natl. Acad. Sci. USA. 102, 3129-3134.
DOI
|
45 |
Desantis, V., Lamanuzzi, A. and Vacca, A. 2018. The role of SIRT6 in tumors. Haematologica 103, 1-4.
DOI
|
46 |
Dharmasiri, N., Dharmasiri, S. and Estelle, M. 2005. The F-box protein TIR1 is an auxin receptor. Nature 435, 441-445.
DOI
|
47 |
Disch, J. S., Evindar, G., Chiu, C. H., Blum, C. A., Dai, H., Jin, L., Schuman, E., Lind, K. E., Belyanskaya, S. L., Deng, J., Coppo, F., Aquilani, L., Graybill, T. L., Cuozzo, J. W., Lavu, S., Mao, C., Vlasuk, G. P. and Perni, R. B. 2013. Discovery of Thieno[3,2-d]pyrimidine-6-carboxamides as Potent Inhibitors of SIRT1, SIRT2, and SIRT3. J. Med. Chem. 56, 3666-3679.
DOI
|
48 |
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 SIRT family of NAD-dependent deacetylases by phenotypic screening. J. Biol. Chem. 276, 38837-38843.
DOI
|
49 |
Hardtke, C. S. and Berleth, T. 1998. The Arabidopsis gene MONOPTEROS encodes a transcription factor mediating embryo axis formation and vascular development. EMBO J. 17, 1405-1411.
DOI
|
50 |
Hawse, W. F., Hoff, K. G., Fatkins, D. G., Daines, A., Zubkova, O. V., Schramm, V. L., Zheng, W. and Wolberger, C. 2008. Structural insights into intermediate steps in the Sir2 deacetylation reaction. Structure 16, 1368-1377.
DOI
|
51 |
He, B., Hu, J., Zhang, X. and Lin, H. 2014. Thiomyristoyl peptides as cell-permeable Sirt6 inhibitors. Org. Biomol. Chem. 12, 7498-7502.
DOI
|
52 |
Heger, V., Tyni, J., Hunyadi, A., Horakova, L., Lahtela-Kakkonen, M. and Rahnasto-Rilla, M. 2019. Quercetin based derivatives as SIRT inhibitors. Biomed. Pharmacother. 111, 1326-1333.
DOI
|
53 |
Chen, B., Zang, W., Wang, J., Huang, Y., He, Y., Yan, L., Liu, J. and Zheng, W. 2015. The chemical biology of SIRTs. Chem. Soc. Rev. 44, 5246-5264.
DOI
|
54 |
Cheng, Y., Dai, X. and Zhao, Y. 2004. AtCAND1, a HEAT-repeat protein that participates in auxin signaling in Arabidopsis. Plant Physiol. 135, 1020-1026.
DOI
|
55 |
Cucurachi, M., Busconi, M., Morreale, G., Zanetti, A., Bavaresco, L. and Fogher, C. 2012. Characterization and differential expression analysis of complete coding sequences of Vitis vinifera L. SIRT genes. Plant Physiol. Biochem. 54, 123-132.
DOI
|
56 |
Cui, H., Kamal, Z., Ai, T., Xu, Y., More, S. S., Wilson, D. J. and Chen, L. 2014. Discovery of potent and selective SIRT 2 (SIRT2) inhibitors using a fragment-based approach. J. Med. Chem. 57, 8340-8357.
DOI
|
57 |
Du, J., Zhou, Y., Su, X., Yu, J. J., Khan, S., Jiang, H., Kim, J., Woo, J., Kim, J. H., Choi, B. H., He, B., Chen, W., Zhang, S., Cerione, R. A., Auwerx, J., Hao, Q. and Lin, H. 2011. Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase. Science 334, 806-809.
DOI
|
58 |
Friden-Saxin, M., Seifert, T., Landergren, M. R., Suuronen, T., Lahtela-Kakkonen, M., Jarho, E. M. and Luthman, K. 2012. Synthesis and evaluation of substituted chroman-4-one and chromone derivatives as SIRT 2-selective inhibitors. J. Med. Chem. 55, 7104-7113.
DOI
|
59 |
Frye, R. A. 1999. Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (SIRTs) metabolize NAD and may have protein ADP-ribosyltransferase activity. Biochem. Biophys. Res. Commun. 260, 273-279.
DOI
|
60 |
Frye, R. A. 2000. Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins. Biochem. Biophys. Res. Commun. 273, 793-798.
DOI
|
61 |
Greiss, S. and Gartner, A. 2009. SIRT/Sir2 phylogeny, evolutionary considerations and structural conservation. Mol. Cells 28, 407-415.
DOI
|
62 |
Peck, B., Chen, C. Y., Ho, K. K., Di Fruscia, P., Myatt, S. S., Coombes, R. C., Fuchter, M. J., Hsiao, C. D. and Lam, E. W. 2010. SIRT inhibitors induce cell death and p53 acetylation through targeting both SIRT1 and SIRT2. Mol. Cancer Ther. 9, 844-855.
DOI
|
63 |
Perabo, F. G. and Muller, S. C. 2005. New agents in intravesical chemotherapy of superficial bladder cancer. Scand. J. Urol. Nephrol. 39, 108-116.
DOI
|
64 |
Pereira, C. V., Lebiedzinska, M., Wieckowski, M. R. and Oliveira, P. J. 2012. Regulation and protection of mitochondrial physiology by SIRTs. Mitochondrion 12, 66-76.
DOI
|
65 |
Heltweg, B., Gatbonton, T., Schuler, A. D., Posakony, J., Li, H., Goehle, S., Kollipara, R., Depinho, R. A., Gu, Y., Simon, J. A. and Bedalov, A. 2006. Antitumor activity of a smallmolecule inhibitor of human silent information regulator 2 enzymes. Cancer Res. 66, 4368-4377.
DOI
|
66 |
Hirai, S., Endo, S., Saito, R., Hirose, M., Ueno, T., Suzuki, H., Yamato, K., Abei, M. and Hyodo, I. 2014. Antitumor effects of a SIRT inhibitor, tenovin-6, against gastric cancer cells via death receptor 5 up-regulation. PLoS One 9, e102831.
DOI
|
67 |
Hollender, C. and Liu, Z. 2008. Histone deacetylase genes in Arabidopsis development. J. Integr. Plant Biol. 50, 875-885.
DOI
|
68 |
Hu, J., Jing, H. and Lin, H. 2014. SIRT inhibitors as anticancer agents. Future Med. Chem. 6, 945-966.
DOI
|
69 |
Perry, J., Dai, X. and Zhao, Y. 2005. A mutation in the anticodon of a single tRNAala is sufficient to confer auxin resistance in Arabidopsis. Plant Physiol. 139, 1284-1290.
DOI
|
70 |
Portmann, S., Fahrner, R., Lechleiter, A., Keogh, A., Overney, S., Laemmle, A., Mikami, K., Montani, M., Tschan, M. P., Candinas, D. and Stroka, D. 2013. Antitumor effect of SIRT1 inhibition in human HCC tumor models in vitro and in vivo. Mol. Cancer Ther. 12, 499-508.
DOI
|
71 |
Preyat, N. and Leo, O. 2013. SIRT deacylases: a molecular link between metabolism and immunity. J. Leukoc. Biol. 93, 669-680.
DOI
|
72 |
Przemeck, G. K., Mattsson, J., Hardtke, C. S., Sung, Z. R. and Berleth, T. 1996. Studies on the role of the Arabidopsis gene MONOPTEROS in vascular development and plant cell axialization. Planta 200, 229-237.
DOI
|
73 |
Pulla, V. K., Alvala, M., Sriram, D. S., Viswanadha, S., Sriram, D. and Yogeeswari, P. 2014. Structure-based drug design of small molecule SIRT1 modulators to treat cancer and metabolic disorders. J. Mol. Graph. Model. 52, 46-56.
DOI
|
74 |
Rack, J. G., Morra, R., Barkauskaite, E., Kraehenbuehl, R., Ariza, A., Qu, Y., Ortmayer, M., Leidecker, O., Cameron, D. R., Matic, I., Peleg, A. Y., Leys, D., Traven, A. and Ahel, I. 2015. Identification of a class of protein ADP-Ribosylating SIRTs in microbial pathogens. Mol. Cell. 59, 309-320.
DOI
|
75 |
Rahnasto-Rilla, M., Tyni, J., Huovinen, M., Jarho, E., Kulikowicz, T., Ravichandran, S., V, A. B., Ferrucci, L., Lahtela-Kakkonen, M. and Moaddel, R. 2018. Natural polyphenols as SIRT 6 modulators. Sci. Rep. 8, 4163.
DOI
|
76 |
Rajabi, N., Galleano, I., Madsen, A. S. and Olsen, C. A. 2018. Targeting SIRTs: substrate specificity and inhibitor design. Prog. Mol. Biol. Transl. Sci. 154, 25-69.
DOI
|
77 |
Rine, J. and Herskowitz, I. 1987. Four genes responsible for a position effect on expression from HML and HMR in Saccharomyces cerevisiae. Genetics 116, 9-22.
DOI
|
78 |
Rotili, D., Tarantino, D., Nebbioso, A., Paolini, C., Huidobro, C., Lara, E., Mellini, P., Lenoci, A., Pezzi, R., Botta, G., Lahtela-Kakkonen, M., Poso, A., Steinkuhler, C., Gallinari, P., De Maria, R., Fraga, M., Esteller, M., Altucci, L. and Mai, A. 2012. Discovery of salermide-related SIRT inhibitors: binding mode studies and antiproliferative effects in cancer cells including cancer stem cells. J. Med. Chem. 55, 10937-10947.
DOI
|
79 |
Rumpf, T., Schiedel, M., Karaman, B., Roessler, C., North, B. J., Lehotzky, A., Olah, J., Ladwein, K. I., Schmidtkunz, K., Gajer, M., Pannek, M., Steegborn, C., Sinclair, D. A., Gerhardt, S., Ovadi, J., Schutkowski, M., Sippl, W., Einsle, O. and Jung, M. 2015. Selective Sirt2 inhibition by ligand-induced rearrangement of the active site. Nat. Commun. 6, 6263.
DOI
|
80 |
Sacconnay, L., Ryckewaert, L., Randazzo, G. M., Petit, C., Passos Cdos, S., Jachno, J., Michailoviene, V., Zubriene, A., Matulis, D., Carrupt, P. A., Simoes-Pires, C. A. and Nurisso, A. 2016. 5-Benzylidene-hydantoin is a new scaffold for SIRT inhibition: From virtual screening to activity assays. Eur. J. Pharm. Sci. 85, 59-67.
DOI
|
81 |
Satoh, A., Brace, C. S., Ben-Josef, G., West, T., Wozniak, D. F., Holtzman, D. M., Herzog, E. D. and Imai, S. 2010. SIRT1 promotes the central adaptive response to diet restriction through activation of the dorsomedial and lateral nuclei of the hypothalamus. J. Neurosci. 30, 10220-10232.
DOI
|
82 |
Schlicker, C., Boanca, G., Lakshminarasimhan, M. and Steegborn, C. 2011. Structure-based development of novel SIRT inhibitors. Aging (Albany NY) 3, 852-872.
DOI
|
83 |
Huang, L., Sun, Q., Qin, F., Li, C., Zhao, Y. and Zhou, D. X. 2007. Down-regulation of a SILENT INFORMATION REGULATOR2-related histone deacetylase gene, OsSRT1, induces DNA fragmentation and cell death in rice. Plant Physiol. 144, 1508-1519.
DOI
|
84 |
Imai, S., Armstrong, C. M., Kaeberlein, M. and Guarente, L. 2000. Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature 403, 795-800.
DOI
|
85 |
Sebastian, C., Zwaans, B. M., Silberman, D. M., Gymrek, M., Goren, A., Zhong, L., Ram, O., Truelove, J., Guimaraes, A. R., Toiber, D., Cosentino, C., Greenson, J. K., MacDonald, A. I., McGlynn, L., Maxwell, F., Edwards, J., Giacosa, S., Guccione, E., Weissleder, R., Bernstein, B. E., Regev, A., Shiels, P. G., Lombard, D. B. and Mostoslavsky, R. 2012. The histone deacetylase SIRT6 is a tumor suppressor that controls cancer metabolism. Cell 151, 1185-1199.
DOI
|
86 |
Shore, D. 2000. The Sir2 protein family: A novel deacetylase for gene silencing and more. Proc. Natl. Acad. Sci. USA. 97, 14030-14032.
DOI
|
87 |
Singh, S., Singh, A., Yadav, S., Gautam, V., Singh, A. and Sarkar, A. K. 2017. Sirtinol, a Sir2 protein inhibitor, affects stem cell maintenance and root development in Arabidopsis thaliana by modulating auxin-cytokinin signaling components. Sci. Rep. 7, 42450.
DOI
|
88 |
Smith, B. C. and Denu, J. M. 2007. Mechanism-based inhibition of Sir2 deacetylases by thioacetyl-lysine peptide. Biochemistry 46, 14478-14486.
DOI
|
89 |
Smith, J. S., Brachmann, C. B., Celic, I., Kenna, M. A., Muhammad, S., Starai, V. J., Avalos, J. L., Escalante-Semerena, J. C., Grubmeyer, C., Wolberger, C. and Boeke, J. D. 2000. A phylogenetically conserved NAD+-dependent protein deacetylase activity in the Sir2 protein family. Proc. Natl. Acad. Sci. USA. 97, 6658-6663.
DOI
|
90 |
Sociali, G., Galeno, L., Parenti, M. D., Grozio, A., Bauer, I., Passalacqua, M., Boero, S., Donadini, A., Millo, E., Bellotti, M., Sturla, L., Damonte, P., Puddu, A., Ferroni, C., Varchi, G., Franceschi, C., Ballestrero, A., Poggi, A., Bruzzone, S., Nencioni, A. and Del Rio, A. 2015. Quinazolinedione SIRT6 inhibitors sensitize cancer cells to chemotherapeutics. Eur. J. Med. Chem. 102, 530-539.
DOI
|
91 |
Jackson, M. D., Schmidt, M. T., Oppenheimer, N. J. and Denu, J. M. 2003. Mechanism of nicotinamide inhibition and transglycosidation by Sir2 histone/protein deacetylases. J. Biol. Chem. 278, 50985-50998.
DOI
|
92 |
Jiang, H., Khan, S., Wang, Y., Charron, G., He, B., Sebastian, C., Du, J., Kim, R., Ge, E., Mostoslavsky, R., Hang, H. C., Hao, Q. and Lin, H. 2013. SIRT6 regulates TNF-alpha secretion through hydrolysis of long-chain fatty acyl lysine. Nature 496, 110-113.
DOI
|
93 |
Jiang, K. and Feldman, L. J. 2005. Regulation of root apical meristem development. Annu. Rev. Cell Dev. Biol. 21, 485-509.
DOI
|
94 |
Jiang, Y., Liu, J., Chen, D., Yan, L. and Zheng, W. 2017. SIRT Inhibition: strategies, inhibitors, and therapeutic potential. Trends Pharmacol. Sci. 38, 459-472.
DOI
|
95 |
Jung-Hynes, B., Nihal, M., Zhong, W. and Ahmad, N. 2009. Role of SIRT histone deacetylase SIRT1 in prostate cancer. A target for prostate cancer management via its inhibition? J. Biol. Chem. 284, 3823-3832.
DOI
|
96 |
Kaluski, S., Portillo, M., Besnard, A., Stein, D., Einav, M., Zhong, L., Ueberham, U., Arendt, T., Mostoslavsky, R., Sahay, A. and Toiber, D. 2017. Neuroprotective functions for the histone deacetylase SIRT6. Cell Rep. 18, 3052-3062.
DOI
|
97 |
Kanfi, Y., Naiman, S., Amir, G., Peshti, V., Zinman, G., Nahum, L., Bar-Joseph, Z. and Cohen, H. Y. 2012. The SIRT SIRT6 regulates lifespan in male mice. Nature 483, 218-221.
DOI
|
98 |
Sussmuth, S. D., Haider, S., Landwehrmeyer, G. B., Farmer, R., Frost, C., Tripepi, G., Andersen, C. A., Di Bacco, M., Lamanna, C., Diodato, E., Massai, L., Diamanti, D., Mori, E., Magnoni, L., Dreyhaupt, J., Schiefele, K., Craufurd, D., Saft, C., Rudzinska, M., Ryglewicz, D., Orth, M., Brzozy, S., Baran, A., Pollio, G., Andre, R., Tabrizi, S. J., Darpo, B., Westerberg, G. and Consortium, P. 2015. An exploratory double-blind, randomized clinical trial with selisistat, a SirT1 inhibitor, in patients with Huntington's disease. Br. J. Clin. Pharmacol. 79, 465-476.
DOI
|
99 |
Suzuki, T., Asaba, T., Imai, E., Tsumoto, H., Nakagawa, H. and Miyata, N. 2009. Identification of a cell-active non-peptide SIRT inhibitor containing N-thioacetyl lysine. Bioorg. Med. Chem. Lett. 19, 5670-5672.
DOI
|
100 |
Suzuki, T., Khan, M. N., Sawada, H., Imai, E., Itoh, Y., Yamatsuta, K., Tokuda, N., Takeuchi, J., Seko, T., Nakagawa, H. and Miyata, N. 2012. Design, synthesis, and biological activity of a novel series of human SIRT-2-selective inhibitors. J. Med. Chem. 55, 5760-5773.
DOI
|
101 |
Szucko, I. 2016. SIRTs: not only animal proteins. Acta Physiol. Plant. 38, 237.
DOI
|
102 |
Tanny, J. C., Dowd, G. J., Huang, J., Hilz, H. and Moazed, D. 1999. An enzymatic activity in the yeast Sir2 protein that is essential for gene silencing. Cell 99, 735-745.
DOI
|
103 |
Tasselli, L., Zheng, W. and Chua, K. F. 2017. SIRT6: novel mechanisms and links to aging and disease. Trends Endocrinol. Metab. 28, 168-185.
DOI
|
104 |
Tromas, A. and Perrot-Rechenmann, C. 2010. Recent progress in auxin biology. C. R. Biol. 333, 297-306.
DOI
|