The DOI matches its Crossref record; 36 of the 36 references it cites were found in a registry or an index.
Ten years of NAD-dependent SIR2 family deacetylases: implications for metabolic diseases
Open accessAbstract
In the past decade since the discovery of NAD-dependent deacetylase activity of the SIR2 (silent information regulator 2) family, now called “sirtuins,” many exciting connections between protein deacetylation and energy metabolism have been revealed. The importance of sirtuins have been firmly established in the regulation of many fundamental biological responses to a variety of nutritional and environmental stimuli. Sirtuins have also emerged as critical regulators for aging and longevity in model organisms. Their absolute requirement of NAD has revived an enthusiasm in the study of mammalian NAD biosynthesis. Furthermore, sirtuin-targeted pharmaceutical and nutriceutical interventions against age-associated diseases are now on the horizon. This review will summarize the recent progress in sirtuin research, particularly in the field of mammalian sirtuin biology, and reevaluate the connection between sirtuins, metabolism, and age-associated diseases, such as type 2 diabetes, to set a milepost for the next 10 years of sirtuin research.
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Citations
Cites
Mechanisms linking obesity to insulin resistance and type 2 diabetes
Kahn, S. E., Hull, R. L., & Utzschneider, K. M. (2006) · Nature · doi:10.1038/nature05482 · Cited by 5,448
Resveratrol improves health and survival of mice on a high-calorie diet
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Small molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan
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Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
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Self-citationNutrient control of glucose homeostasis through a complex of PGC-1α and SIRT1
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Self-citationImpaired Mitochondrial Activity in the Insulin-Resistant Offspring of Patients with Type 2 Diabetes
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Sirtuin activators mimic caloric restriction and delay ageing in metazoans
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Self-citation
Cited by
Sirt5 Is a NAD-Dependent Protein Lysine Demalonylase and Desuccinylase
Du, J., Zhou, Y., Su, X., Yu, J. J., Khan, S., Jiang, H., Kim, J., Woo, J., Kim, J. H., Choi, B. H., et al. (2011) · Science · doi:10.1126/science.1207861 · Cited by 1,429
Yoshino, J., Mills, K. F., Yoon, M. J., & Imai, S.-I. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.08.014 · Cited by 1,340
Self-citationLiu, T. F., Vachharajani, V. T., Yoza, B. K., & McCall, C. E. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.362343 · Cited by 340
SIRT7 represses Myc activity to suppress ER stress and prevent fatty liver disease
Shin, J., He, M., Liu, Y., Paredes, S., Villanova, L., Brown, K., Qiu, X., Nabavi, N., Mohrin, M., Wojnoonski, K., et al. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.10.007 · Cited by 287
“The sirtuin family of nicotinamide adenine dinucleotide (NAD+)-dependent deacetylases is profoundly implicated in metabolic regulation (Bellet et al., 2012; Finkel et al., 2009; Gillum et al.; Hirschey et al., 2011; Houtkooper et al.; Imai and Guarente, 2010).”
BackgroundA SIRT7-Dependent Acetylation Switch of GABPβ1 Controls Mitochondrial Function
Ryu, D., Jo, Y. S., Lo Sasso, G., Stein, S., Zhang, H., Perino, A., Lee, J. U., Zeviani, M., Romand, R., Hottiger, M. O., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.08.001 · Cited by 263
Metadata
- Authors
- Imai, S.-I., & Guarente, L.
- Venue
- Trends in Pharmacological Sciences
- Publisher
- Elsevier BV
- Published
- 2010-05
- Volume
- 31
- Issue
- 5
- Pages
- 212-220
- ISSN
- 0165-6147 (ISSN-L)
- OpenAlex
- W2019548769
- Cited by
- 390
- References
- 36
- FWCI
- 3.16
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Imai, S.-I., & Guarente, L. (2010). Ten years of NAD-dependent SIR2 family deacetylases: implications for metabolic diseases. Trends in Pharmacological Sciences. https://doi.org/10.1016/j.tips.2010.02.003
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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