Nutritional biomarkers: Current view and future perspectives

References

• Alp Ikizler, T. (2012). The use and misuse of serum albumin as a nutritional marker in kidney disease. Clin. J. Am. Soc. Nephrol. 7:1375–1377.
   PubMed Web of Science ®Google Scholar
• Andersen, H. U., Fey, S. J., Larsen, P. M., Nawrocki, A., Hejnaes, K. R., Mandrup–Poulsen, T. and Nerup, J. (1997). Interleukin-1 beta induced changes in the protein expression of rat islets: A computerised database. Electrophoresis 18:2091–2103.
   PubMed Web of Science ®Google Scholar
• Bajoub, A., Bendini, A., Fernández–gutiÉrrez, A. and Carrasco–Pancorbo, A. (2016). Olive oil authentication: A comparative analysis of regulatory frameworks with especial emphasis on quality and authenticity indices, and recent analytical techniques developed for their assessment– a review. Crit. Rev. Food Sci. Nutr. Doi:10.1080/10408398.2016.1225666.
   PubMed Web of Science ®Google Scholar
• Banh, L. (2006). Serum proteins as markers of nutrition: What are we treating? Prac. Gastroenterol. 46:46–64.
   Google Scholar
• Baur, J. A., Pearson, K. J., Price, N. L., Jamieson, H. A., Lerin, C., Kalra, A., Prabhu, V. V, Allard, J. S., Lopez-Lluch, G., Lewis, K., Pistell, P. J., Poosala, S., Becker, K. G., Boss, O., Gwinn, D., Wang, M., Ramaswamy, S., Fishbein, K. W., Spencer, R. G., Lakatta, E. G., Le Couteur, D., Shaw, R. J., Navas, P., Puigserver, P., Ingram, D. K., de Cabo, R., Sinclair, D. A. (2006). Resveratrol improves health and survival of mice on a high-calorie diet. Nature 444:337–342.
   PubMed Web of Science ®Google Scholar
• Bayram, B., Ozcelik, B. S., Grimm Roeder, T., Schrader, C., Ernst, I. M., Wagner, A. E., Grune, T., Frank, J. and Rimbach, G. (2012). A diet rich in olive oil phenolics reduces oxidative stress in the heart of SAMP8 mice by induction of Nrf2–dependent gene expression. Rejuvenation Res. 15:71–81.
   PubMed Web of Science ®Google Scholar
• Beck, F. K. and Rosenthal, T. C. (2002). Prealbumin: A marker for nutritional evaluation. Am. Fam. Physician 65:1575–1578.
   PubMed Web of Science ®Google Scholar
• Bell, E. L., Emerling, B. M., Ricoult, S. J. H. and Guarente, L. (2011). SirT3 suppresses hypoxia inducible factor 1α and tumor growth by inhibiting mitochondrial ROS production. Oncogene 30:2986–2996.
   PubMed Web of Science ®Google Scholar
• Bordone, L. and Guarente, L. (2005). Calorie restriction, SIRT1 and metabolism: Understanding longevity. Nat. Rev. Mol. Cell Biol. 6:298–305.
   PubMed Web of Science ®Google Scholar
• Borra, M. T., Smith, B. C. and Denu, J. M. (2005). Mechanism of human SIRT1 activation by resveratrol. J. Biol. Chem. 280:17187–17195.
   PubMed Web of Science ®Google Scholar
• Borra, M. T. and Denu, J. M. (2004). Quantitative assays for characterization of the Sir2 family of NAD +-dependent deacetylases. Methods Enzymol. 376:171–187.
   PubMed Web of Science ®Google Scholar
• Bradbury, C. A., Khanim, F. L., Hayden, R., Bunce, C. M., White, D. A, Drayson, M. T., Craddock, C. and Turner, B. M. (2005). Histone deacetylases in acute myeloid leukaemia show a distinctive pattern of expression that changes selectively in response to deacetylase inhibitors. Leukemia 19:1751–1759.
   PubMed Web of Science ®Google Scholar
• Brooks, C. L. and Gu, W. (2010). How does SIRT1 affect metabolism, senescence and cancer? Nat. Rev. Cancer 9:123–128.
   Web of Science ®Google Scholar
• Budayeva, H. G., Rowland, E. A. and Cristea, I. M. (2016). Intricate roles of mammalian sirtuins in defense against viral pathogens. J. Virol. 90:5–8.
   PubMed Web of Science ®Google Scholar
• Calabrese, V., Cornelius, C., Leso, V., Trovato-Salinaro, A., Ventimiglia, B., Cavallaro, M., Scuto, M., Rizza, S., Zanoli, L., Neri, S. and Castellino, P. (2012). Oxidative stress, glutathione status, sirtuin and cellular stress response in type 2 diabetes. Biochim. Biophys. Acta 1822:729–36.
   PubMed Web of Science ®Google Scholar
• Castro, R. E., Ferreira, D. M. S., Afonso, M. B., Borralho, P. M., MacHado, M. V., Cortez-Pinto, H. and Rodrigues, C. M. P. (2013). MiR-34a/SIRT1/p53 is suppressed by ursodeoxycholic acid in the rat liver and activated by disease severity in human non-alcoholic fatty liver disease. J. Hepatol. 58:119–125.
   PubMed Web of Science ®Google Scholar
• Chalkiadaki, A. and Guarente, L. (2012). Sirtuins mediate mammalian metabolic responses to nutrient availability. Nat. Rev. Endocrinol. 8:287–296.
   PubMed Web of Science ®Google Scholar
• Chong, Z. Z. and Maiese, K. (2008). Enhanced tolerance against early and late apoptotic oxidative stress in mammalian neurons through nicotinamidase and sirtuin mediated pathways. Curr. Neurovasc. Res. 5:159–70.
   PubMed Web of Science ®Google Scholar
• Choudhary, C., Weinert, B. T., Nishida, Y., Verdin, E. and Mann, M. (2014). The growing landscape of lysine acetylation links metabolism and cell signalling. Nat. Rev. Mol. Cell Biol. 15:536–550.
   PubMed Web of Science ®Google Scholar
• Cohen, D. E., Supinski, A. M., Bonkowski, M. S., Donmez, G. and Guarente, L. P. (2009). Neuronal SIRT1 regulates endocrine and behavioral responses to calorie restriction. Genes Dev. 23:2812–2817.
   PubMed Web of Science ®Google Scholar
• Combs, G. F., Trumbo, P. R., Mckinley, M. C., Milner, J., Studenski, S., Kimura, T., Watkin, S. M. and Raiten, D. J. (2013). Biomarkers in nutrition: New frontiers in research and application. Ann. NY. Acad. Sci. 1278:1–10.
   PubMed Web of Science ®Google Scholar
• de Roos, B. and McArdle, H. J. (2008). Proteomics as a tool for the modelling of biological processes and biomarker development in nutrition research. Br. J. Nutr. 99:66–71.
   PubMed Web of Science ®Google Scholar
• Dang, W., Steffen, K. K., Perry, R., Dorsey, J. A., Johnson, F. B., Shilatifard, A., Kaeberlein, M., Kennedy, B. K. and Berger, S. L. (2009). Histone H4 lysine 16 acetylation regulates cellular lifespan. Nature. 459:802–807.
   PubMed Web of Science ®Google Scholar
• Dominy, J. E. Jr, Lee, Y., Gerhart–Hines, Z. and Puigserver, P. (2010). Nutrient–dependent regulation of PGC–1alpha's acetylation state and metabolic function through the enzymatic activities of Sirt1/GCN5. Biochim. Biophys. Acta 1804:1676–1683.
   PubMed Web of Science ®Google Scholar
• Don, B. R. and Kaysen, G. (2004). Serum albumin: Relationship to inflammation and nutrition. Semin. Dial. 17:432–437.
   PubMed Web of Science ®Google Scholar
• Erion, D. M., Yonemitsu, S., Nie, Y., Nagai, Y., Gillum, M. P., Hsiao, J. J., Iwasaki, T., Stark, R., Weismann, D., Yu, X. X., Murray, S. F., Bhanot, S., Monia, B. P., Horvath, T. L., Gao, Q., Samuel, V. T. and Shulman, G. I. (2009). SirT1 knockdown in liver decreases basal hepatic glucose production and increases hepatic insulin responsiveness in diabetic rats. Proc. Natl. Acad. Sci. U. S. A. 106:11288–11293.
   PubMed Web of Science ®Google Scholar
• Fan, Y., Ludewig, R. and Scriba, G. K. E. (2009). 9-Fluorenylmethoxycarbonyl-labeled peptides as substrates in a capillary electrophoresis-based assay for sirtuin enzymes. Anal. Biochem. 387:243–248.
   PubMed Web of Science ®Google Scholar
• Ferguson, L. R. (2001). Role of plant polyphenols in genomic stability. Mutat. Res. 18:89–111.
   Web of Science ®Google Scholar
• Finley, L. W. S., Carracedo, A., Lee, J., Souza, A., Egia, A., Zhang, J., Teruya-Feldstein, J., Moreira, P. I., Cardoso, S. M., Clish, C. B., Pandolfi, P. P. and Haigis, M. C. (2011). SIRT3 opposes reprogramming of cancer cell metabolism through HIF1alpha destabilization. Cancer Cell 19:416–428.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• Frye, R. A. (1999). Characterization of five human cDNAs with homology to the yeast SIR2 gene. Biochem. Biophys. Res. Commum. 260:273–279.
   PubMed Web of Science ®Google Scholar
• Frye, R. A. (2000). Phylogenetic classification of prokaryotic and eukaryotic Sir2–like proteins. Biochem. Biophys. Res. Commun. 273:793–798.
   PubMed Web of Science ®Google Scholar
• Fuchs, D., Winkelmann, I., Johnson, I. T., Mariman, E., Wenzel, U. and Daniel, H. (2005). Proteomics in nutrition research: Principles, technologies and applications. Br. J. Nutr. 94:302–314.
   PubMed Web of Science ®Google Scholar
• Gambini, J., Gomez-Cabrera, M. C., Borras, C., Valles, S. L., Lopez-Grueso, R., Martinez-Bello, V. E., Herranz, D., Pallardo, F. V., Tresguerres, J. A. F., Serrano, M. and Viña, J. (2011). Free [NADH]/[NAD+] regulates sirtuin expression. Arch. Biochem. Biophys. 512:24–29.
   PubMed Web of Science ®Google Scholar
• Gertz, M. and Steegborn, C. (2010). Function and regulation of the mitochondrial Sirtuin isoform Sirt5 in Mammalia. Biochim. Biophys. Acta 1804:1658–1665.
   PubMed Web of Science ®Google Scholar
• Gibson, R. S. (2005). Measuring food composition in individuals In: Principles of Nutritional Assessment, pp. 41–64. Gibson, R. S., Eds., 2nd edition, Oxford University Press, New York.
   Google Scholar
• Grabowska, W., Suszek, M., Wnuk, M., Lewinska, A., Wasiak, E., Sikora, E. and Bielak–Zmijewska, A. (2016). Curcumin elevates sirtuin level but does not postpone in vitro senescence of human cells building the vasculature. Oncotarget. 7, Doi: 10.18632/oncotarget8450.
   Web of Science ®Google Scholar
• Grbesa, I., Pajares, M. J., Martínez-Terroba, E., Agorreta, J., Mikecin, A. M., Larráyoz, M., Idoate, M. A., Gall-Troselj, K., Pio, R. and Montuenga, L. M. (2015). Expression of sirtuin 1 and 2 is associated with poor prognosis in non-small cell lung cancer patients. PLoS One 10:1–17.
   Web of Science ®Google Scholar
• Greiss, S. and Gartner, A. (2009). Sirtuin/Sir2 phylogeny, evolutionary considerations and structural conservation. Mol. Cells 28:407–415.
   PubMed Web of Science ®Google Scholar
• Guarente, L. (2000). Sir2 links chromatin silencing, metabolism, and aging. Genes Dev. 14:1021–1026.
   PubMed Web of Science ®Google Scholar
• Guarente, L. (2006). Sirtuins as potential targets for metabolic syndrome. Nature 444:868–874.
   PubMed Web of Science ®Google Scholar
• Guarente, L. (2014). Linking DNA damage, NAD+/SIRT1, and aging. Cell Metab. 20:706–707.
   PubMed Web of Science ®Google Scholar
• Gygi, S. P., Corthals, G. L., Zhang, Y., Rochon, Y. and Aebersold, R. (2000). Evaluation of two-dimensional gel electrophoresis based proteome analysis technology. Proc. Natl. Acad. Sci. U. S. A. 97:9390–9395.
   PubMed Web of Science ®Google Scholar
• Hafner, A. V., Dai, J., Gomes, A. P., Xiao, C. Y., Palmeira, K. C. M., Rosenzweig, A. and Sinclair, D. A. (2010). Regulation of the mPTP by SIRT3-mediated deacetylation of CypD at lysine 166 suppresses age-related cardiac hypertrophy. Aging (Albany. NY). 2:914–923.
   PubMedGoogle Scholar
• Hagopian, K., Ramsey, J. J. and Weindruch, B. (2009). Caloric restriction counteracts age–related changes in the activities of sorbitol metabolizing enzymes from mouse liver. Biogerontology 10:471–479.
   PubMed Web of Science ®Google Scholar
• Haigis, M. C. and Sinclair, D. A. (2010). Mammalian sirtuins: Biological insights and disease relevance. Annu. Rev. Pathol. 5:253–295.
   PubMed Web of Science ®Google Scholar
• Haigis, M. C., Mostoslavsky, R., Haigis, K. M., Fahie, K., Christodoulou, D. C., Murphy, A. J., Valenzuela, D. M., Yancopoulos, G. D., Karow, M., Blander, G., Wolberger, C., Prolla, T. A., Weindruch, R., Alt, F. W. and Guarente, L. (2006). SIRT4 inhibits glutamate dehydrogenase and opposes the effects of calorie restriction in pancreatic beta cells. Cell 126:941–954.
   PubMed Web of Science ®Google Scholar
• Harikumar, K. B. and Aggarwal, B. B. (2008). Resveratrol: A multitargeted agent for age-associated chronic diseases. Cell Cycle 7:1020–1037.
   PubMed Web of Science ®Google Scholar
• Hasegawa, K., Wakino, S., Yoshioka, K., Tatematsu, S., Hara, Y., Minakuchi, H., Washida, N., Tokuyama, H., Hayashi, K. and Itoh, H. (2008). Sirt1 protects against oxidative stress-induced renal tubular cell apoptosis by the bidirectional regulation of catalase expression. Biochem. Biophys. Res. Commun. 372:51–56.
   PubMed Web of Science ®Google Scholar
• Hauffman, D. M., Grizzle, W. E., Bamman, M. M., Kim, J. S., Eltoum, I. A., Elgavish, A. and Nagy, T. R. (2007). SIRT1 is significantly elevated in mouse and human prostate cancer. Cancer Res. 67:6612–6618.
   PubMed Web of Science ®Google Scholar
• Hedrick, V. E., Dietrich, A. M., Estabrooks, P. A., Savla, J., Serrano, E. and Davy, B. M. (2012). Dietary biomarkers: Advances, limitations and future directions. Nutr. J. 11:109–113.
   PubMed Web of Science ®Google Scholar
• Heltweg, B., Dequiedt, F., Verdin, E. and Jung, M. (2003). Nonisotopic substrate for assaying both human zinc and NAD+-dependent histone deacetylases. Anal. Biochem. 319:42–48.
   PubMed Web of Science ®Google Scholar
• Herranz, D. and Serrano, M. (2013). Sirt1: Recent lessons from mouse models. Nat. Rev. Cancer 10:819–823.
   Web of Science ®Google Scholar
• Herranz, D., Muñoz-Martin, M., Cañamero, M., Mulero, F., Martinez-Pastor, B., Fernandez-Capetillo, O. and Serrano, M. (2010). Sirt1 improves healthy ageing and protects from metabolic syndrome-associated cancer. Nat. Commun. 1:3.
   PubMed Web of Science ®Google Scholar
• Hirschey, M. D., Shimazu, T., Capra, J. A., Pollard, K. S. and Verdin, E. (2011). SIRT1 and SIRT3 deacetylate homologous substrates. Aging 3:635–642.
   PubMedGoogle Scholar
• Hishida, T., Nozaki, Y., Nakachi, Y., Mizuno, Y., Iseki, H., Katano, M., Kamon, M., Hirasaki, M., Nishimoto, M., Okazaki, Y. and Okuda, A. (2012). Sirt1, p53, and p38MAPK are crucial regulators of detrimental phenotypes of embryonic stem cells with Max expression ablation. Stem Cells 30:1634–1644.
   PubMed Web of Science ®Google Scholar
• Hochberg, I. and Hochberg, Z. (2009). Hypothalamic obesity. Endocrine Dev. 17:185–196.
   PubMedGoogle Scholar
• Hou, X., Xu, S., Maitland-Toolan, K. A., Sato, K., Jiang, B., Ido, Y., Lan, F., Walsh, K., Wierzbicki, M., Verbeuren, T. J., Cohen, R. A. and Zang, M. (2008). SIRT1 regulates hepatocyte lipid metabolism through activating AMP-activated protein kinase. J. Biol. Chem. 283:20015–20026.
   PubMed Web of Science ®Google Scholar
• Howitz, K., Bitterman, J. and Cohen, H. (2003). Small molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan. Nature 425:191–196.
   PubMed Web of Science ®Google Scholar
• Hulka, B. S. (1993). Overview of biological markers In: Biological Markers in Epidemiology, pp. 3–15. Hulka, B. S., Wilcosky, T. C., and Griffin, J. D., Eds., Oxford University Press, New york.
   Google Scholar
• Kaaks, R., Riboli, E. and Sinha, R. (1997). Biochemical markers of dietary intake In: Application of Biomarkers in Cancer Epidemiology, pp. 103–126. Toniolo, P., Boffetta, P, Shuker, D. E. G., Rothman, N., Hulka, B. and Pearce, N., Eds., IARC Scientific Publications No. 142, International Agency for Research on Cancer, Lyons, France.
   Google Scholar
• Kaeberlein, M., McDonagh, T., Heltweg, B., Hixon, J., Westman, E. A., Caldwell, S. D., Napper, A., Curtis, R., DiStefano, P. S., Fields, S., Bedalov, A. and Kennedy, B. K. (2005). Substrate-specific activation of sirtuins by resveratrol. J. Biol. Chem. 280:17038–17045.
   PubMed Web of Science ®Google Scholar
• Kaidi, A., Weinert, B. T., Choudhary, C. and Jackson, S. P. (2010). Human SIRT6 promotes DNA end resection through CtIP deacetylation. Science 329:1348–1353.
   PubMed Web of Science ®Google Scholar
• Kanfi, Y., Shalman, R., Peshti, V., Pilosof, S. N., Gozlan, Y. M., Pearson, K. J., Lerrer, B., Moazed, D., Marine, J. C., de Cabo, R. and Cohen, H. Y. (2008). Regulation of SIRT6 protein levels by nutrient availability. FEBS Lett. 582:543–548.
   PubMed Web of Science ®Google Scholar
• Kanfi, Y., Naiman, S., Amir, G., Peshti, V., Zinman, G., Nahum, L., Bar-Joseph, Z. and Cohen, H. Y. (2012). The sirtuin SIRT6 regulates lifespan in male mice. Nature 483:218–221.
   PubMed Web of Science ®Google Scholar
• Kawahara, T. L., Michishita, E., Adler, A. S., Damian, M., Berber, E., Lin, M., McCord, R. A., Ongaigui, K. C., Boxer, L. D., Chang, H. Y. and Chua, K. F. (2009). SIRT6 links histone H3 lysine 9 deacetylation to NF-kappaB-dependent gene expression and organismal life span. Cell 136:62–74.
   PubMed Web of Science ®Google Scholar
• Kennedy, B. K., Gotta, M., Sinclair, D. A., Mills, K, David, S. M., Mala, M., Pak, S. M., Laroche, T., Gasser, S. M. and Guarenteet, L. (1997). Redistribution of silencing proteins from telomeres to the nucleolus is associated with extension of life span in S. cerevisiae. Cell 89:381–391.
   PubMed Web of Science ®Google Scholar
• Koyuncu, E., Budayeva, H. G., Miteva, Y. V., Ricci, D. P., Silhavy, T. J., Shenk, T. and Cristea, I. M. (2014). Sirtuins are evolutionarily conserved viral restriction factors. MBio 5:1–10.
   Web of Science ®Google Scholar
• Kuhnle, G. G. C. (2012). Nutritional biomarkers for objective dietary assessment. J. Sci. Food Agric. 92:1145–1149.
   PubMed Web of Science ®Google Scholar
• Kume, S., Uzu, T., Kashiwagi, A. and Koya, D. (2010). SIRT1, a calorie restriction mimetic, in a new therapeutic approach for type 2 diabetes mellitus and diabetic vascular complications. Endocr. Metab. Immune Disord. Drug Targets 10:16–24.
   PubMedGoogle Scholar
• Kuzuya, M., Izawa, S., Enoki, H., Okada, K. and Iguchi, A. (2007). Is serum albumin a good marker for malnutrition in the physically impaired elderly? Clin. Nutr. 26:84–90.
   PubMed Web of Science ®Google Scholar
• Laurent, G., de Boer, V. C. J., Finley, L. W. S., Sweeney, M., Lu, H., Schug, T. T., Cen, Y., Jeong, S. M., Li, X., Sauve, A. A. and Haigis, M. C. (2013). SIRT4 represses peroxisome proliferator-activated receptor activity to suppress hepatic fat oxidation. Mol. Cell. Biol. 33:4552–4561.
   PubMed Web of Science ®Google Scholar
• Li, X. (2013). SIRT1 and energy metabolism. Acta Biochim. Biophys. Sin. 45:51–60.
   Google Scholar
• Li, X. and Kazgan, N. (2011). Mammalian sirtuins and energy metabolism. Int. J. Biol. Sci. 7:575–587.
   PubMed Web of Science ®Google Scholar
• Li, Y., Xu, R., Zhang, X. M., Li, D. D. and He, Q. Y. (2008). Mechanism of apoptosis induced by SIRT1 deacetylase inhibitors in human breast cancer MCF–7 drug–resistant cells. Yao Xue Xue Bao 43:1003–1010.
   PubMedGoogle Scholar
• Liu, T. F., Vachharajani, V. T., Yoza, B. K. and McCall, C. E. (2012). NAD+ -dependent sirtuin 1 and 6 proteins coordinate a switch from glucose to fatty acid oxidation during the acute inflammatory response. J. Biol. Chem. 287:25758–25769.
   PubMed Web of Science ®Google Scholar
• Liu, Y., Gerber, R., Wu, J., Tsuruda, T., McCarter, J. D. (2008). High-throughput assays for sirtuin enzymes: A microfluidic mobility shift assay and a bioluminescence assay. Anal. Biochem. 378:53–59.
   PubMed Web of Science ®Google Scholar
• Lomb, D. J., Laurent, G. and Haigis, M. C. (2010). Sirtuins regulate key aspects of lipid metabolism. Biochim. Biophys. Acta 1804:1652–1657.
   PubMed Web of Science ®Google Scholar
• Lundby, C. and Olsen, J. V. (2012). Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns. Cell Rep. 2:419–431.
   PubMed Web of Science ®Google Scholar
• 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 107:137–48.
   PubMed Web of Science ®Google Scholar
• Maiese, K., Chong, Z. Z., Shang, Y. C. and Hou, J. (2009). A “FOXO” in sight: Targeting Foxo proteins from conception to cancer. Med. Res. Rev. 29:395–418.
   PubMed Web of Science ®Google Scholar
• Mao, Z., Hine, C., Tian, X., Van Meter, M., Au, M., Vaidya, A., Seluanov, A. and Gorbunova, V. (2011). SIRT6 promotes DNA repair under stress by activating PARP1. Science 332:1443–1446.
   PubMed Web of Science ®Google Scholar
• Marcotte, P. A., Richardson, P. R., Guo, J., Barrett, L. W., Xu, N., Gunasekera, A. and Glaser, K. B. (2004). Fluorescence assay of SIRT protein deacetylases using an acetylated peptide substrate and a secondary trypsin reaction. Anal. Biochem. 332:90–99.
   PubMed Web of Science ®Google Scholar
• Martínez-Redondo, P. and Vaquero, A. (2013). The diversity of histone versus nonhistone sirtuin substrates. Genes Cancer 4:148–63.
   PubMedGoogle Scholar
• McDonagh, T., Hixon, J., DiStefano, P. S., Curtis, R. and Napper, A. D. (2005). Microplate filtration assay for nicotinamide release from NAD using a boronic acid resin. Methods 36:346–350.
   PubMed Web of Science ®Google Scholar
• Menendez, J. A., Joven, J., Aragonès, G., Barrajón-Catalán, E., Beltrán-Debón, R., Borrás-Linares, I., Camps, J., Corominas-Faja, B., Cufí, S., Fernández-Arroyo, S., Garcia-Heredia, A., Hernández-Aguilera, A., Herranz-López, M., Jiménez-Sánchez, C., López-Bonet, E., Lozano-Sánchez, J., Luciano-Mateo, F., Martin-Castillo, B., Martin-Paredero, V., Pérez-Sánchez, A., Oliveras-Ferraros, C., Riera-Borrull, M., Rodríguez-Gallego, E., Quirantes-Piné, R., Rull, A., Tomás-Menor, L., Vazquez-Martin, A., Alonso-Villaverde, C., Micol, V. and Segura-Carretero, A. (2013). Xenohormetic and anti-aging activity of secoiridoid polyphenols present in extra virgin olive oil: A new family of gerosuppressant agents. Cell Cycle 12:555–578.
   PubMed Web of Science ®Google Scholar
• Michan, S. and Sinclair, D. (2007). Sirtuins in mammals: Insights into their biological function. Biochem. J. 15(404):1–13.
   Web of Science ®Google Scholar
• Michishita, E., McCord, R. A., Berber, E., Kioi, M., Padilla‐Nash, H., Damian, M., Cheung, P., Kusumoto, R., Kawahara, T. L., Barrett, J. C., Chang, H. Y. Bohr, Y. A. and Ried, T. (2005b). SIRT6 is a histone H3 lysine 9 deacetylase that modulates telomeric chromatin. Nature 452:492–496.
   Web of Science ®Google Scholar
• Michishita, E., McCord, R. A., Berber, E., Kioi, M., Padilla-Nash, H., Damian, M., Cheung, P., Kusumoto, R., Kawahara, T. L. A., Barrett, J. C., Chang, H. Y., Bohr, V. A., Ried, T., Gozani, O. and Chua, K. F. (2008). SIRT6 is a histone H3 lysine 9 deacetylase that modulates telomeric chromatin. Nature 452:492–496.
   PubMed Web of Science ®Google Scholar
• Michishita, E., Park, J. Y., Burneskis, J. M., Barrett, J. C. and Horikawa, I. (2005a). Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins. Mol. Biol. Cell 16:4623–4635.
   PubMed Web of Science ®Google Scholar
• Miroslava, C. and Adrian, S. C. (2014). Role of histone deacetylases in fungal phytopathogenesis: A review. Int. J. Modern Botany 4:48–60.
   Google Scholar
• Mischak, H., Allmaier, G., Apweiler, R., Attwood, T., Baumann, M., Benigni, A., Bennett, S. E., Bischoff, R., Bongcam-Rudloff, E., Capasso, G., Coon, J. J., D'Haese, P., Dominiczak, A. F., Dakna, M., Dihazi, H., Ehrich, J. H., Fernandez-Llama, P., Fliser, D., Frokiaer, J., Garin, J., Girolami, M., Hancock, W. S., Haubitz, M., Hochstrasser, D., Holman, R. R., Ioannidis, J. P. A., Jankowski, J., Julian, B. A., Klein, J. B., Kolch, W., Luider, T., Massy, Z., Mattes, W. B., Molina, F., Monsarrat, B., Novak, J., Peter, K., Rossing, P., Sánchez-Carbayo, M., Schanstra, J. P., Semmes, O. J., Spasovski, G., Theodorescu, D., Thongboonkerd, V., Vanholder, R., Veenstra, T. D., Weissinger, E., Yamamoto, T. and Vlahou, A. (2010). Recommendations for biomarker identification and qualification in clinical proteomics. Sci. Transl. Med. 2:42–45.
   Web of Science ®Google Scholar
• Morris, B. J. (2013). Seven sirtuins for seven deadly diseases ofaging. Free Radic. Biol. Med. 56:133–171.
   PubMed Web of Science ®Google Scholar
• Morselli, E., Maiuri, M. C., Markaki, M., Megalou, E., Pasparaki, A., Palikaras, K., Criollo, A., Galluzzi, L., Malik, S. a, Vitale, I., Michaud, M., Madeo, F., Tavernarakis, N. and Kroemer, G. (2010). Caloric restriction and resveratrol promote longevity through the Sirtuin-1-dependent induction of autophagy. Cell Death Dis. 21:1–11.
   Google Scholar
• Mostoslavsky, R., Chua, K. F., Lombard, D. B., Pang, W. W., Fisher, M. R., Gellon, L., Liu, P., Mostoslavsky, G., Franco, S. and Murphy, M. M. (2006). Cell 124:315–329.
   PubMed Web of Science ®Google Scholar
• Muller, P. A. J. and Vousden, K. H. (2013). p53 mutations in cancer. Nat. Cell Biol. 15:2–8.
   PubMed Web of Science ®Google Scholar
• Nadtochiy, S. M., Urciuoli, W., Zhang, J., Schafer, X., Munger, J. and Brookes, P. S. (2015). Metabolomic profiling of the heart during acute ischemic preconditioning reveals a role for SIRT1 in rapid cardioprotective metabolic adaptation. J. Mol. Cell. Cardiol. 88:64–72.
   PubMed Web of Science ®Google Scholar
• Nakagawa, T., Lomb, D. J., Haigis, M. C. and Guarente, L. (2009). SIRT5 deacetylates carbamoyl phosphate synthetase 1 and regulates the urea cycle. Cell 137:560–570.
   PubMed Web of Science ®Google Scholar
• Nasrin, N., Wu, X., Fortier, E., Feng, Y., Baré, O. C., Chen, S., Ren, X., Wu, Z., Streeper, R. S. and Bordone, L. (2010). SIRT4 regulates fatty acid oxidation and mitochondrial gene expression in liver and muscle cells. J. Biol. Chem. 285:31995–32002.
   PubMed Web of Science ®Google Scholar
• Nemoto, S., Fergusson, M. M. and Finkel, T. (2004). Nutrient availability regulates SIRT1 through a fork head dependent pathway. Science 306:2105–2108.
   PubMed Web of Science ®Google Scholar
• Nemoto, S., Fergusson, M. M. and Finkel, T. (2005). SIRT1 functionally interacts with the metabolic regulator and transcriptional coactivator PGC-1α. J. Biol. Chem. 280(16):16456–16460.
   PubMed Web of Science ®Google Scholar
• Nie, Y., Erion, D., Yuan, Z., Dietrich, M., Shulman, G., Horvath, T. and Gao, Q. (2009). STAT3 inhibition of gluconeogenesis is downregulated by SirT1. Nat. Cell. Biol. 11:492–500.
   PubMed Web of Science ®Google Scholar
• Nikiforov, A., Kulikova, V. and Ziegler, M. (2015). The human NAD metabolome: Functions, metabolism and compartmentalization. Crit. Rev. Biochem. Mol. Biol. 50:284–297.
   PubMed Web of Science ®Google Scholar
• Nogueiras, R., Habegger, K. M., Chaudhary, N., Finan, B., Banks, A. S., Dietrich, M. O., Horvath, T. L., Sinclair, D. A., Pfluger, P. T. and Tschop, M. H. (2012). Sirtuin 1 and sirtuin 3: Physiological modulators of metabolism. Physiol. Rev. 92:1479–1514.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• North, B. J. and Verdin, E. (2004). Sirtuins: Sir2-related NAD-dependent protein deacetylases. Genome biol. 5(5):224.
   PubMed Web of Science ®Google Scholar
• Oellerich, M. F. and Potente, M. (2012). FOXOs and sirtuins in vascular growth, maintenance, and aging. Circ. Res. 110:1238–1251.
   PubMed Web of Science ®Google Scholar
• Osborne, T. F. and Espenshade, P. J. (2009). Evolutionary conservation and adaptation in the mechanism that regulates SREBP action: What a long, strange tRIP it's been. Genes Dev. 23:2578–2591.
   PubMed Web of Science ®Google Scholar
• 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. 3:0210–0220.
   Web of Science ®Google Scholar
• Pallàs, M., Pizarro, J. G., Gutierrez-Cuesta, J., Crespo-Biel, N., Alvira, D., Tajes, M., Yeste-Velasco, M., Folch, J., Canudas, A. M., Sureda, F. X., Ferrer, I. and Camins, A. (2008). Modulation of SIRT1 expression in different neurodegenerative models and human pathologies. Neuroscience 154:1388–1397.
   PubMed Web of Science ®Google Scholar
• Pallauf, K., Giller, K., Huebbe, P. and Rimbach, G. (2013). Nutrition and healthy ageing: Calorie restriction or polyphenol-rich “mediterrAsian” diet? Oxid. Med. Cell. Longev. 2013:14–28.
   Web of Science ®Google Scholar
• Pande, S. and Srinivasan, K. (2012). Potentiation of hypolipidemic and weight–reducing influence of dietary tender cluster bean (Cyamopsis tetragonoloba) when combined with capsaicin in high–fat–fed rats. J. Agri. Food Chem. 60:8155–8162.
   PubMed Web of Science ®Google Scholar
• Pande, S. and Srinivasan, K. (2013). Protective effect of dietary tender cluster beans (Cyamopsis tetragonoloba) in the gastrointestinal tract of experimental rats. Appl. Physiol. Nutr. Metab. 38:169–176.
   PubMed Web of Science ®Google Scholar
• Pérez, V. I., Bokov, A., Remmen, H. Van, Mele, J., Ran, Q., Ikeno, Y. and Richardson, A. (2009). Is the oxidative stress theory of aging dead? Biochim. Biophys. Acta 1790:1005–1014.
   PubMed Web of Science ®Google Scholar
• Pfluger, P. T., Herranz, D., Velasco-Miguel, S., Serrano, M. and Tschop, M. H. (2008). Sirt1 protects against high-fat diet-induced metabolic damage. Proc. Natl. Acad. Sci. U. S. A. 105:9793–9798.
   PubMed Web of Science ®Google Scholar
• Picard, F., Kurtev, M., Chung, N., Topark-Ngarm, A., Senawong, T., Machado De Oliveira, R., Leid, M., McBurney, M. W. and Guarente, L. (2004). Sirt1 promotes fat mobilization in white adipocytes by repressing PPAR-gamma. Nature 429:771–776.
   PubMed Web of Science ®Google Scholar
• Ponugoti, B., Kim, D. H., Xiao, Z., Smith, Z., Miao, J., Zang, M., Wu, S. Y., Chiang, C. M., Veenstra, T. D. and Kemper, J. K. (2010). SIRT1 deacetylates and inhibits SREBP-1C activity in regulation of hepatic lipid metabolism. J. Biol. Chem. 285:33959–33970.
   PubMed Web of Science ®Google Scholar
• Potischman, N. (2003). Biologic and methodologic issues for nutritional biomarkers. J. Nutr. 133:875S–880S.
   PubMed Web of Science ®Google Scholar
• Priyanka, A., Solanki, V., Parkesh, R. and Thakur, K. G. (2016). Crystal structure of the N-terminal domain of human SIRT7 reveals a three-helical domain architecture. Proteins Struct. Funct. Bioinforma. 1–6. Doi:10.1002/prot.25085
   Web of Science ®Google Scholar
• Prozorovski, T., Schulze-Topphoff, U., Glumm, R., Baumgart, J., Schröter, F., Ninnemann, O., Siegert, E., Bendix, I., Brüstle, O., Nitsch, R., Zipp, F. and Aktas, O. (2008). Sirt1 contributes critically to the redox-dependent fate of neural progenitors. Nat. Cell Biol. 10:385–94.
   PubMed Web of Science ®Google Scholar
• Purushotham, A., Xu, Q., Lu, J., Foley, J. F., Yan, X., Kim, D. H. and Kemper, J. K. (2012). Hepatic deletion of SIRT1 decreases hepatocyte nuclear factor 1alpha/farnesoid X receptor signaling and induces formation of cholesterol gallstones in mice. Mol. Cell. Biol. 32:1226–1236.
   PubMed Web of Science ®Google Scholar
• Purushotham, A., Schug, T. T., Xu, Q., Surapureddi, S., Guo, X. and Li, X. (2009). Hepatocyte–specific deletion of SIRT1 alters fatty acid metabolism and results in hepatic steatosis and inflammation. Cell Metab. 9:327–38.
   PubMed Web of Science ®Google Scholar
• Qiu, X., Brown, K., Hirschey, M. D., Verdin, E. and Chen, D. (2010). Calorie restriction reduces oxidative stress by SIRT3–mediated SOD2 activation. Cell. Metab. 1:662–667.
   Web of Science ®Google Scholar
• Rajapakse, N. and Kim, S. K. (2011). Nutritional and digestive health benefits of seaweed. Adv. Food. Nutr. Res. 64:17–28.
   PubMedGoogle Scholar
• Rasbach, K. A. and Schnellmann, R. G. (2008). Isoflavones promote mitochondrial biogenesis. J. Pharmacol. Exp. Ther. 325:536–543.
   PubMed Web of Science ®Google Scholar
• Rauh, D., Fischer, F., Gertz, M., Lakshminarasimhan, M., Bergbrede, T., Aladini, F., Kambach, C., Becker, C. F. W., Zerweck, J., Schutkowski, M. and Steegborn, C. (2013). An acetylome peptide microarray reveals specificities and deacetylation substrates for all human sirtuin isoforms. Nat. Commun. 4:2327.
   PubMed Web of Science ®Google Scholar
• Ren, J. H., Tao, Y., Zhang, Z. Z., Chen, W.-X., Cai, X. F., Chen, K., Ko, B. C. B., Song, C.-L., Ran, L. K., Li, W. Y., Huang, A. L. and Chen, J. (2014). Sirtuin 1 regulates hepatitis B virus transcription and replication by targeting transcription factor AP-1. J. Virol. 88:2442–2451.
   PubMed Web of Science ®Google Scholar
• Reny, J. L., Vuagnat, A., Ract, C., Benoit, M. O., Safar, M. and Fagon, J. Y. (2002). Diagnosis and follow-up of infections in intensive care patients: Value of C-reactive protein compared with other clinical and biological variables. Crit. Care Med. 30:529–535.
   PubMed Web of Science ®Google Scholar
• Rimbach, G., Boesch-Saadatmandi, C., Frank, J., Fuchs, D., Wenzel, U., Daniel, H., Hall, W. L. and Weinberg, P. D. (2008). Dietary isoflavones in the prevention of cardiovascular disease - A molecular perspective. Food Chem. Toxicol. 46:1308–1319.
   PubMed Web of Science ®Google Scholar
• Rodgers, J. T. and Puigserver, P. (2007). Fasting-dependent glucose and lipid metabolic response through hepatic sirtuin 1. Proc. Natl. Acad. Sci. U. S. A. 104:12861–1286.
   PubMed Web of Science ®Google Scholar
• Rodgers, J. T., Lerin, C., Haas, W., Gygi, S. P., Spiegelman, B. M. and Puigserver, P. (2005). Nutrient control of glucose homeostasis through a complex of PGC-1a and SIRT1. Nature 434:113–118.
   PubMed Web of Science ®Google Scholar
• Rogina, B. and Helfand, S. L. (2004). Sir2 mediates longevity in the fly through a pathway related to calorie restriction. Proc. Natl. Acad. Sci. 101:5998–6003.
   PubMed Web of Science ®Google Scholar
• Rui, L. (2014). Energy metabolism in the liver. Compr. Physiol. 4:177–197.
   PubMed Web of Science ®Google Scholar
• Sadhukhan, S., Liu, X., Ryu, D., Nelson, O. D., Stupinski, J. A., Li, Z., Chen, W., Zhang, S., Weiss, R. S., Locasale, J. W., Auwerx, J. and Lin, H. (2016). Metabolomics-assisted proteomics identifies succinylation and SIRT5 as important regulators of cardiac function. Proc. Natl. Acad. Sci. 113:201519858. Doi:10.1073/pnas.1519858113
   Web of Science ®Google Scholar
• Schlicker, C., Gertz, M., Papatheodorou, P., Kachholz, B., Becker, C. F. W. and Steegborn, C. (2008). Substrates and regulation mechanisms for the human mitochondrial sirtuins Sirt3 and Sirt5. J. Mol. Biol. 382:790–801.
   PubMed Web of Science ®Google Scholar
• Schug, T. T., Xu, Q., Gao, H., Peres–da–Silva, A., Draper, D. W., Fessler, M. B., Purushotham, A. and Li, X. (2010). Myeloid deletion of SIRT1 induces inflammatory signaling in response to environmental stress. Mol. Cell Biol. 30:4712–4721.
   PubMed Web of Science ®Google Scholar
• Schug, T. T. and Li, X. (2011). Sirtuin 1 in lipid metabolism and obesity. Ann. Med. 43:198–211.
   PubMed Web of Science ®Google Scholar
• Schuster, S., Roessler, C., Meleshin, M., Zimmermann, P., Simic, Z., Kambach, C., Schiene-Fischer, C., Steegborn, C., Hottiger, M. O. and Schutkowski, M. (2016). A continuous sirtuin activity assay without any coupling to enzymatic or chemical reactions. Sci. Rep. 6:22643.
   PubMed Web of Science ®Google Scholar
• Schwer, B. and Verdin, E. (2008). Conserved Metabolic Regulatory Functions of Sirtuins. Cell Metab. 7:104–112.
   PubMed Web of Science ®Google Scholar
• Simó-Mirabet, P., Bermejo-Nogales, A., Calduch-Giner, J. A. and Pérez-Sánchez, J. (2016). Tissue-specific gene expression and fasting regulation of sirtuin family in gilthead sea bream (Sparus aurata). J. Comp. Physiol. B. 187, Doi:10.1007/s00360-016-1014-0.
   PubMed Web of Science ®Google Scholar
• Sinclair, D. A. and Guarente, L. (2006). Unlocking the secrets of longevity genes. Sci. Am. 294:48–57.
   PubMed Web of Science ®Google Scholar
• Sohal, R. S. and Weindruch, R. (1996). Oxidative stress, caloric restriction, and aging. Science 273:59–63.
   PubMed Web of Science ®Google Scholar
• Someya, S., Yu, W., Hallows, W. C., Xu, J., Vann, J. M., Leeuwenburgh, C., Tanokura, M., Denu, J. M. and Prolla, T. A. (2010). Sirt3 mediates reduction of oxidative damage and prevention of age–related hearing loss under caloric restriction. Cell 143:802–812.
   PubMed Web of Science ®Google Scholar
• Spiekerman, A. M. (1995). Nutritional assessment (protein nutrition). Anal. Chem. 67:29–36.
   Web of Science ®Google Scholar
• Suresh, D. and Srinivasan, K. (2010). Tissue distribution & elimination of capsaicin, piperine & curcumin following oral intake in rats. Indian J. Med. Res. 131:682–691.
   PubMed Web of Science ®Google Scholar
• Tanno, M., Kuno, A., Yano, T., Miura, T., Hisahara, S., Ishikawa, S., Shimamoto, K. and Horio, Y. (2010). Induction of manganese superoxide dismutase by nuclear translocation and activation of SIRT1 promotes cell survival in chronic heart failure. J. Biol. Chem. 285:8375–8382.
   PubMed Web of Science ®Google Scholar
• Tao, R., Coleman, M. C., Pennington, J. D., Ozden, O., Park, S. H., Jiang, H., Kim, H. S., Flynn, C. R., Hill, S., McDonald, W. H., Olivier, A. K., Spitz, D. R. and Gius, D. (2010). Sirt3-mediated deacetylation of evolutionarily conserved lysine 122 regulates MnSOD activity in response to stress. Mol. Cell 40:893–904.
   PubMed Web of Science ®Google Scholar
• Tarantino, G., Finelli, C., Scopacasa, F., Pasanisi, F., Contaldo, F., Capone, D. and Savastano, S. (2014). Circulating levels of sirtuin 4, a potential marker of oxidative metabolism, related to coronary artery disease in obese patients suffering from nafld, with normal or slightly increased liver enzymes. Oxid. Med. Cell. Longev. 9:1–10.
   Web of Science ®Google Scholar
• Tissenbaum, H. A. and Guarente, L. (2001). Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans. Nature 410:227–230.
   PubMed Web of Science ®Google Scholar
• Trayhurn, P. (2000). Proteomics and nutrition – a science for the first decade of the new millennium. Br. J. Nutr. 83:1–2.
   PubMed Web of Science ®Google Scholar
• Vachharajani, V. T., Liu, T., Wang, X., Hoth, J. J., Yoza, B. K. and McCall, C. E. (2016). Sirtuins link inflammation and metabolism. J. Immunol. Res. 2016, doi:10.1155/2016/8167273.
   PubMedGoogle Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• Walker, A. K., Yang, F., Jiang, K., Ji, J. Y., Watts, J. L., Purushotham, A., Boss, O., Hirsch, M. L., Ribich, S., Smith, J. J., Israelian, K., Westphal, C. H., Rodgers, J. T., Shioda, T., Elson, S. L., Mulligan, P., Najafi-Shoushtari, H., Black, J. C., Thakur, J. K., Kadyk, L. C., Whetstine, J. R., Mostoslavsky, R., Puigserver, P., Li, X., Dyson, N. J., Hart, A. C. and Näär, A. M. (2010). Conserved role of SIRT1 orthologs in fasting-dependent inhibition of the lipid/cholesterol regulator SREBP. Genes Dev. 24:1403–1417.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• Wang, T. J., Gona, P., Larson, M. G., Tofler, G. H., Levy, D., Newton-Cheh, C., Jacques, P. F., Rifai, N., Selhub, J., Robins, S. J., Benjamin, E. J., D'Agostino, R. B. and Vasan, R. S. (2006). Multiple biomarkers for the prediction of first major cardiovascular events and death. N. Engl. J. Med. 355:2631–2639.
   PubMed Web of Science ®Google Scholar
• Wang, W., McReynolds, M. R., Goncalves, J. F., Shu, M., Dhondt, I., Braeckman, B. P., Lange, S. E., Kho, K., Detwiler, A. C., Pacella, M. J. and Hanna-Rose, W. (2015). Comparative metabolomic profiling reveals that dysregulated glycolysis stemming from lack of salvage NAD+ biosynthesis impairs reproductive development in Caenorhabditis elegans. J. Biol. Chem. 290:26163–26179.
   PubMed Web of Science ®Google Scholar
• Wegener, D., Hildmann, C., Riester, D., Schwienhorst, A. (2003). Improved fluorogenic histone deacetylase assay for high-throughput-screening applications. Anal. Biochem. 321:202–208.
   PubMed Web of Science ®Google Scholar
• Yoshizaki, T., Schenk, S., Imamura, T., Babendure, J. L., Sonoda, N., Bae, E. J., Oh, D. Y., Lu, M., Milne, J. C., Westphal, C., Bandyopadhyay, G. and Olefsky, J. M. (2010). SIRT1 inhibits inflammatory pathways in macrophages and modulates insulin sensitivity. Am. J. Physiol. Endocrinol. Metab. 298:E419–E428.
   PubMed Web of Science ®Google Scholar
• Zhang, S. and Wang, X. I. (2013). SIRT1 is a useful biomarker for high-grade dysplasia and carcinoma in barrett's esophagus. Ann. Clin. Lab. Sci. 43:373–377.
   PubMed Web of Science ®Google Scholar
• Zhang, T. and Kraus, W. L. (2010). SIRT1-dependent regulation of chromatin and transcription: Linking NAD+ metabolism and signaling to the control of cellular functions. Biochim. Biophys. Acta - Proteins Proteomics 1804:1666–1675.
   PubMed Web of Science ®Google Scholar
• Zhao, K., Chai, X. and Marmorstein, R. (2004). Structure and substrate binding properties of cobB, a Sir2 homolog protein deacetylase from Escherichia coli. J. Mol. Biol. 337:731–741.
   PubMed Web of Science ®Google Scholar
• Zhao, S., Xu, W., Jiang, W. Yu, W., Lin, Y., Zhang, T., Yao, J., Zhou, L., Zeng, Y., Li, H., Li, Y., Shi, J., An, W., Hancock, S. M., He, F., Qin, L., Chin, J., Yang, P., Chen, X., Lei, Q., Xiong, Y. and Guan, K. L. (2010). Regulation of cellular metabolism by protein lysine acetylation. Science 327:1000–1004.
   PubMed Web of Science ®Google Scholar
• Ziemke, F. and Mantzoros, C. S. (2010). Adiponectin in insulin resistance: Lessons from translational research. Am. J. Clin. Nutr. 91:258–261.
   PubMed Web of Science ®Google Scholar