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NAD+ and sirtuins in aging and disease
Open accessAbstract
Nicotinamide adenine dinucleotide (NAD(+)) is a classical coenzyme mediating many redox reactions. NAD(+) also plays an important role in the regulation of NAD(+)-consuming enzymes, including sirtuins, poly-ADP-ribose polymerases (PARPs), and CD38/157 ectoenzymes. NAD(+) biosynthesis, particularly mediated by nicotinamide phosphoribosyltransferase (NAMPT), and SIRT1 function together to regulate metabolism and circadian rhythm. NAD(+) levels decline during the aging process and may be an Achilles' heel, causing defects in nuclear and mitochondrial functions and resulting in many age-associated pathologies. Restoring NAD(+) by supplementing NAD(+) intermediates can dramatically ameliorate these age-associated functional defects, counteracting many diseases of aging, including neurodegenerative diseases. Thus, the combination of sirtuin activation and NAD(+) intermediate supplementation may be an effective antiaging intervention, providing hope to aging societies worldwide.
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“The NAMPT (nicotinamide phosphoribosyltransferase) protein and NAD+ levels decreased significantly in organs, such as white adipose tissue and skeletal muscle in old mice [13] affecting the activity of NAD+ -dependent enzymes such as sirtuins [15, 98].”
From NAD+ Precursors Nicotinamide Mononucleotide (NMN) and Nicotinamide Riboside (NR): Potential Dietary Contribution to Health (2023) · cites this paper as [15]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“During the aging process, DNA damage accumulates in the cell nucleus causing PARPs activation and reducing both NAD+ levels and SIRT1 activity [15].”
From NAD+ Precursors Nicotinamide Mononucleotide (NMN) and Nicotinamide Riboside (NR): Potential Dietary Contribution to Health (2023) · cites this paper as [15]
Experimental — accuracy not yet measuredIn the citing paper
“several studies have proposed that PARP1 inhibition can be used to promote increases in cellular levels of NAD+ by decreasing its degradation”
From A Potent and Specific CD38 Inhibitor Ameliorates Age-Related Metabolic Dysfunction by Reversing Tissue NAD+ Decline (2018) · cites this paper as Imai and Guarente, 2014
In the citing paper
“PARP1 is the main PARP enzyme in mammalian tissues and utilize NAD+ during its catalysis”
From A Potent and Specific CD38 Inhibitor Ameliorates Age-Related Metabolic Dysfunction by Reversing Tissue NAD+ Decline (2018) · cites this paper as Imai and Guarente, 2014
In the citing paper
“have been implicated in the regulation of chromosomal integrity, DNA damage repair, metabolism, aging, health span, and longevity”
From A Potent and Specific CD38 Inhibitor Ameliorates Age-Related Metabolic Dysfunction by Reversing Tissue NAD+ Decline (2018) · cites this paper as Imai and Guarente, 2014
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“Sirtuins are enzymes that remove specific covalent modification in lysine residues, such as acetylation, malonylation, and succinylation, in several proteins”
From A Potent and Specific CD38 Inhibitor Ameliorates Age-Related Metabolic Dysfunction by Reversing Tissue NAD+ Decline (2018) · cites this paper as Imai and Guarente, 2014
In the citing paper
“Sirtuin activity and NAD levels both decline with age116,117.”
From Ageing and rejuvenation of tissue stem cells and their niches (2023) · cites this paper as [116]
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2 retracted
RETRACTED: SIRT1 Suppresses β-Amyloid Production by Activating the α-Secretase Gene ADAM10
Dönmez, G., Wang, D., Cohen, D. E., & Guarente, L. (2010) · Cell · doi:10.1016/j.cell.2010.06.020 · Cited by 443
Self-citationRetractedSIRT1 Protects against α-Synuclein Aggregation by Activating Molecular Chaperones
Dönmez, G., Arun, A., Chung, C. Y., McLean, P. J., Lindquist, S. L., & Guarente, L. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.3442-11.2012 · Cited by 208
Self-citationRetractedTranscriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
Imai, S.-I., Armstrong, C. M., Kaeberlein, M., & Guarente, L. (2000) · Nature · doi:10.1038/35001622 · Cited by 3,510
Self-citationStress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase
Brunet, A., Sweeney, L. B., Sturgill, J. F., Chua, K. F., Greer, P. L., Lin, Y., Tran, H., Ross, S. E., Mostoslavsky, R., Cohen, H. Y., et al. (2004) · Science · doi:10.1126/science.1094637 · Cited by 3,239
Nutrient control of glucose homeostasis through a complex of PGC-1α and SIRT1
Rodgers, J. T., Lerin, C., Haas, W., Gygi, S. P., Spiegelman, B. M., & Puigserver, P. (2005) · Nature · doi:10.1038/nature03354 · Cited by 3,160
Kaeberlein, M., McVey, M., & Guarente, L. (1999) · Genes & Development · doi:10.1101/gad.13.19.2570 · Cited by 2,253
Self-citationMammalian Sirtuins: Biological Insights and Disease Relevance
Haigis, M. C., & Sinclair, D. A. (2010) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev.pathol.4.110807.092250 · Cited by 2,085
Lin, S.-J., Defossez, P.-A., & Guarente, L. (2000) · Science · doi:10.1126/science.289.5487.2126 · Cited by 1,775
Self-citationIncreased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans
Tissenbaum, H. A., & Guarente, L. (2001) · Nature · doi:10.1038/35065638 · Cited by 1,603
Self-citationGomes, A. P., Price, N. L., Ling, A. J. Y., Moslehi, J. J., Montgomery, M. K., Rajman, L., White, J. P., Teodoro, J. S., Wrann, C. D., Hubbard, B. P., et al. (2013) · Cell · doi:10.1016/j.cell.2013.11.037 · Cited by 1,482
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Rogina, B., & Tissenbaum, H. A. (2024) · Frontiers in Genetics · doi:10.3389/fgene.2024.1393181 · Cited by 93
Frederick, D. W., Davis, J. G., Dávila, A., Agarwal, B., Michán, S., Puchowicz, M. A., Nakamaru‐Ogiso, E., & Baur, J. A. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.579565 · Cited by 91
Neelakantan, H., Brightwell, C. R., Graber, T. G., Maroto, R., Wang, H.-Y. L., McHardy, S. F., Papaconstantinou, J., Fry, C. S., & Watowich, S. J. (2019) · Biochemical Pharmacology · doi:10.1016/j.bcp.2019.02.008 · Cited by 76
Extracellular NAD+ enhances PARP-dependent DNA repair capacity independently of CD73 activity
Wilk, A. M., Hayat, F., Cunningham, R., Li, J., Garavaglia, S., Zamani, L., Ferraris, D. M., Sýkora, P., Andrews, J., Clark, J., et al. (2020) · Scientific Reports · doi:10.1038/s41598-020-57506-9 · Cited by 91
Yuan, X., Liu, Y., Bijonowski, B. M., Tsai, A., Fu, Q., Logan, T. M., Ma, T., & Li, Y. (2020) · Communications Biology · doi:10.1038/s42003-020-01514-y · Cited by 89
Sirtuins in atherosclerosis: guardians of healthspan and therapeutic targets
Grootaert, M. O. J., & Bennett, M. R. (2022) · Nature Reviews Cardiology · doi:10.1038/s41569-022-00685-x · Cited by 88
Targeting SIRT1 Rescues Age- and Obesity-Induced Microvascular Dysfunction in Ex Vivo Human Vessels
Mengozzi, A., Costantino, S., Paneni, F., Duranti, E., Nannipieri, M., Mancini, R., Lai, M., Rocca, V. L., Puxeddu, I., Antonioli, L., et al. (2022) · Circulation Research · doi:10.1161/circresaha.122.320888 · Cited by 89
SIRT6 is a key regulator of mitochondrial function in the brain
Smirnov, D., Eremenko, E., Stein, D., Kaluski, S., Jasińska, W., Cosentino, C., Martínez-Pastor, B., Brotman, Y., Mostoslavsky, R., Khrameeva, E. E., et al. (2023) · Cell Death and Disease · doi:10.1038/s41419-022-05542-w · Cited by 88
Qin, K., Han, C., Zhang, H., Li, T., Li, N., & Cao, X. (2017) · Journal of Autoimmunity · doi:10.1016/j.jaut.2017.04.006 · Cited by 89
NAMPT as a Therapeutic Target against Stroke
Wang, P., & Miao, C. (2015) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2015.08.012 · Cited by 87
SIRT3 Deacetylates Ceramide Synthases
Novgorodov, S. A., Riley, C. L., Keffler, J. A., Yu, J., Kindy, M. S., Macklin, W. B., Lombard, D. B., & Gudz, T. I. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.668228 · Cited by 86
Poljšak, B., & Milisav, I. (2016) · Rejuvenation Research · doi:10.1089/rej.2015.1767 · Cited by 88
Salminen, A., Kaarniranta, K., & Kauppinen, A. (2016) · Biogerontology · doi:10.1007/s10522-016-9655-7 · Cited by 89
Wei, C., Kong, Y., Hua, X., Li, G., Zheng, S., Cheng, M., Wang, P., & Miao, C. (2017) · British Journal of Pharmacology · doi:10.1111/bph.13979 · Cited by 85
The role of sirtuin 1 in ageing and neurodegenerative disease: A molecular perspective
Thapa, R., Moglad, E. H. O., Afzal, M., Gupta, G., Bhat, A. A., Almalki, W. H., Kazmi, I. A., Alzarea, S. I., Pant, K., Singh, T. G., et al. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102545 · Cited by 87
Kumar, P., Osahon, O. W., & Sekhar, R. V. (2022) · Nutrients · doi:10.3390/nu14051114 · Cited by 83
Epidermal SIRT1 regulates inflammation, cell migration, and wound healing
Qiang, L., Sample, A., Liu, H., Wu, X., & He, Y. (2017) · Scientific Reports · doi:10.1038/s41598-017-14371-3 · Cited by 84
Antioxidant Alternatives in the Treatment of Amyotrophic Lateral Sclerosis: A Comprehensive Review
Carrera‐Juliá, S., Moreno, M. L., Barrios, C., Ortí, J. E. D. L. R., & Drehmer, E. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.00063 · Cited by 87
Adipose tissue NAD + biology in obesity and insulin resistance: From mechanism to therapy
Yamaguchi, S., & Yoshino, J. (2017) · BioEssays · doi:10.1002/bies.201600227 · Cited by 86
Cellular Senescence and Vascular Disease: Novel Routes to Better Understanding and Therapy
Yin, H., & Pickering, J. G. (2016) · Canadian Journal of Cardiology · doi:10.1016/j.cjca.2016.02.051 · Cited by 82
Uddin, G. M., Youngson, N. A., Doyle, B. M., Sinclair, D. A., & Morris, M. J. (2017) · Scientific Reports · doi:10.1038/s41598-017-14866-z · Cited by 82
Mateuszuk, Ł., Campagna, R., Kutryb-Zając, B., Kuś, K., Słominska, E. M., Smolenski, R. T., & Chlopicki, S. (2020) · Biochemical Pharmacology · doi:10.1016/j.bcp.2020.114019 · Cited by 81
SIRT7: the seventh key to unlocking the mystery of aging
Raza, U., Tang, X., Liu, Z., & Liu, B. (2023) · Physiological Reviews · doi:10.1152/physrev.00044.2022 · Cited by 82
Valente, S., Mellini, P., Spallotta, F., Carafa, V., Nebbioso, A., Polletta, L., Carnevale, I., Saladini, S., Trisciuoglio, D., Gabellini, C., et al. (2015) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b01117 · Cited by 80
Korotchkina, L. G., Kazyulkin, D. N., Komarov, P. G., Polinsky, A., Andrianova, E. L., Joshi, S. P., Gupta, M., Vujcic, S., Kononov, E., Toshkov, I. A., et al. (2020) · Leukemia · doi:10.1038/s41375-019-0692-5 · Cited by 81
NAMPT: A critical driver and therapeutic target for cancer
Gasparrini, M., & Audrito, V. (2022) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2022.106189 · Cited by 81
Soncini, D., Caffa, I., Zoppoli, G. M., Cea, M., Cagnetta, A., Passalacqua, M., Mastracci, L., Boero, S., Montecucco, F., Sociali, G., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.594721 · Cited by 79
Tang, S., Fang, Y., Huang, G., Xu, X., Padilla‐Banks, E., Fan, W., Xu, Q., Sanderson, S. M., Foley, J. F., Dowdy, S., et al. (2017) · The EMBO Journal · doi:10.15252/embj.201796708 · Cited by 81
才原一浩, Kamikubo, R., Ikemoto, K., Uchida, K., & Akagawa, M. (2017) · Biochemistry · doi:10.1021/acs.biochem.7b01185 · Cited by 79
Meyer‐Ficca, M. L., & Kirkland, J. B. (2016) · Advances in Nutrition · doi:10.3945/an.115.011239 · Cited by 78
Paoli, A., & Cerullo, G. (2023) · Antioxidants · doi:10.3390/antiox12051065 · Cited by 79
Role and Therapeutic Potential of Astrocytes in Amyotrophic Lateral Sclerosis
Pehar, M., Harlan, B. A., Killoy, K. M., & Vargas, M. R. (2018) · Current Pharmaceutical Design · doi:10.2174/1381612823666170622095802 · Cited by 84
Mikkelsen, K., & Apostolopoulos, V. (2018) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-981-13-2835-0_15 · Cited by 84
Bheereddy, P., Yerra, V. G., Kalvala, A. K., Sherkhane, B., & Kumar, A. (2020) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-020-00923-1 · Cited by 77
Kim, M., Seol, J., Sato, T., Fukamizu, Y., Sakurai, T., & Okura, T. (2022) · Nutrients · doi:10.3390/nu14040755 · Cited by 77
Ergothioneine and its congeners: anti-ageing mechanisms and pharmacophore biosynthesis
Chen, L., Zhang, L., Ye, X., Deng, Z., & Zhao, C. (2023) · Protein & Cell · doi:10.1093/procel/pwad048 · Cited by 78
Role of nutraceutical SIRT1 modulators in AMPK and mTOR pathway: Evidence of a synergistic effect
Giovannini, L., & Bianchi, S. E. (2016) · Nutrition · doi:10.1016/j.nut.2016.09.008 · Cited by 79
Nicotinamide Adenine Dinucleotide Metabolism and Neurodegeneration
Pehar, M., Harlan, B. A., Killoy, K. M., & Vargas, M. R. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7145 · Cited by 77
Mao, K., Chen, J., Yu, H., Li, H., Ren, Y., Wu, X. G., Wen, Y., Zou, F., & Li, W. (2020) · Aging Cell · doi:10.1111/acel.13163 · Cited by 76
Interaction between epigenetic and metabolism in aging stem cells
Brunet, A., & Rando, T. A. (2017) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2016.12.009 · Cited by 79
Hosseini, L., Vafaee, M. S., & Badalzadeh, R. (2019) · Journal of Cardiovascular Pharmacology and Therapeutics · doi:10.1177/1074248419882002 · Cited by 76
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Aguilar‐Arnal, L., Ranjit, S., Stringari, C., Orozco-Solís, R., Gratton, E., & Sassone‐Corsi, P. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1609227113 · Cited by 78
Yu, H., Gan, D., Luo, Z., Yang, Q., An, D., Zhang, H., Hu, Y., Ma, Z., Zeng, Q., Xu, D., et al. (2024) · Molecular Medicine · doi:10.1186/s10020-024-00783-1 · Cited by 76
Lahiguera, Á., Hyroššová, P., Figueras, A., Garzón, D., Moreno‐Justicia, R., Soto‐Cerrato, V., McNeish, I. A., Serra, V., Lázaro, C., Barretina-Ginesta, M.-P., et al. (2020) · EMBO Molecular Medicine · doi:10.15252/emmm.201911217 · Cited by 77
Cardioprotection by nicotinamide mononucleotide (NMN): Involvement of glycolysis and acidic pH
Nadtochiy, S. M., Wang, Y. T., Nehrke, K. W., Munger, J., & Brookes, P. S. (2017) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2018.06.007 · Cited by 75
Moon, Y. J., Zhang, Z., Bang, I. H., Kwon, O. K., Yoon, S., Kim, J. R., Lee, S., Bae, E. J., & Park, B. (2019) · Cell Death and Differentiation · doi:10.1038/s41418-019-0306-9 · Cited by 74
Hu, L., Guo, Y., Song, L., Wen, H., Sun, N., Wang, Y., Qi, B., Liang, Q., Geng, J., Liu, X., et al. (2022) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2022.03.012 · Cited by 73
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Yin, J., Gao, G., Liu, X., Hao, Z.-Q., Li, K., Kang, X.-L., Li, H., Shan, Y., Hu, W., Li, H., et al. (2017) · Nature · doi:10.1038/nature24463 · Cited by 73
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Kruse, S. E., Karunadharma, P. P., Basisty, N., Johnson, R. S., Beyer, R. P., MacCoss, M. J., Rabinovitch, P. S., & Marcinek, D. J. (2015) · Aging Cell · doi:10.1111/acel.12412 · Cited by 73
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Gloston, G. F., Yoo, S. H., & Chen, Z. (2017) · Frontiers in Neurology · doi:10.3389/fneur.2017.00100 · Cited by 73
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Loring, H. S., & Thompson, P. R. (2019) · Cell chemical biology · doi:10.1016/j.chembiol.2019.11.002 · Cited by 76
Ruggieri, S., Orsomando, G., Sorci, L., & Raffaelli, N. (2015) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2015.02.021 · Cited by 71
Chandrasekaran, K., Salimian, M., Konduru, S. R., Choi, J., Kumar, P., Long, A., Klimova, N., Ho, C.-Y., Kristián, T., & Russell, J. W. (2019) · Brain · doi:10.1093/brain/awz324 · Cited by 72
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Zhang, J., Deng, Y., Zhang, M., Su, H., & Qu, Q. (2016) · Neurochemical Research · doi:10.1007/s11064-016-1892-2 · Cited by 70
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Shakespear, M. R., Iyer, A., Cheng, C. Y., Gupta, K. D., Singhal, A., Fairlie, D. P., & Sweet, M. J. (2018) · Trends in Immunology · doi:10.1016/j.it.2018.02.009 · Cited by 70
Harlan, B. A., Killoy, K. M., Pehar, M., Liu, L., Auwerx, J. H., & Vargas, M. R. (2020) · Experimental Neurology · doi:10.1016/j.expneurol.2020.113219 · Cited by 71
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Farr, J. N., & Almeida, M. (2018) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.3564 · Cited by 70
Wyman, A. E., Noor, Z., Fishelevich, R., Lockatell, V., Shah, N. G., Todd, N. W., & Atamas, S. P. (2017) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00473.2016 · Cited by 70
Jadeja, R. N., Powell, F. L., Jones, M. A., Fuller, J., Joseph, E., Thounaojam, M. C., Bartoli, M., & Martin, P. M. (2018) · Aging · doi:10.18632/aging.101469 · Cited by 69
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Kato, M., & Lin, S.-J. (2014) · DNA repair · doi:10.1016/j.dnarep.2014.07.009 · Cited by 71
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Sociali, G., Grozio, A., Caffa, I., Schuster, S., Becherini, P., Damonte, P., Sturla, L., Fresia, C., Passalacqua, M., Mazzola, F., et al. (2018) · The FASEB Journal · doi:10.1096/fj.201800321r · Cited by 68
Gan, H., Shen, T., Chupp, D. P., Taylor, J. R., Sanchez, H. N., Li, X., Xu, Z., Zan, H., & Casali, P. (2020) · Science Advances · doi:10.1126/sciadv.aay2793 · Cited by 71
Kovács, Z., Brunner, B., & Ari, C. (2021) · Nutrients · doi:10.3390/nu13072197 · Cited by 68
Freeberg, K. A., Udovich, C. C., Martens, C. R., Seals, D. R., & Craighead, D. H. (2023) · The Journals of Gerontology Series A · doi:10.1093/gerona/glad106 · Cited by 69
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Tower, J. (2014) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2014.10.008 · Cited by 68
Zhang, M., & Ying, W. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7445 · Cited by 70
Hosseini, L., Farokhi-Sisakht, F., Badalzadeh, R., Khabbaz, A., Mahmoudi, J., & Sadigh‐Eteghad, S. (2019) · Neuroscience · doi:10.1016/j.neuroscience.2019.09.037 · Cited by 66
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Koczor, C. A., Saville, K. M., Andrews, J., Clark, J., Fang, Q., Li, J., Al‐Rahahleh, R. Q., Ibrahim, M., McClellan, S. B., Makarov, M. V., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109917 · Cited by 67
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Bagul, P. K., Dinda, A. K., & Banerjee, S. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.10.126 · Cited by 65
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Luís, C., Maduro, A. I., Pereira, P. M. D. C. C., Mendes, J. J., Soares, R. A., & Ramalho, R. (2022) · Frontiers in Nutrition · doi:10.3389/fnut.2022.958563 · Cited by 64
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Yuan, Q., Zhan, L., Zhou, Q., Zhang, L., Chen, X.-M., Hu, X., & Yuan, X. (2015) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2015.07.045 · Cited by 64
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Chen, H., Wang, S., Zhang, H., Nice, E. C., & Huang, C. (2016) · Expert Review of Anticancer Therapy · doi:10.1080/14737140.2016.1190649 · Cited by 64
Metabolic Syndrome and the Cellular Phase of Alzheimer's Disease
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Metadata
- Authors
- Imai, S.-I., & Guarente, L.
- Affiliations
- Washington University in St. Louis (US)
- Koch Institute for Integrative Cancer Research At MIT (US)
- Corresponding author
- Imai, Shin-ichiro
- Guarente, Leonard
- Venue
- Trends in Cell Biology
- Publisher
- Elsevier BV
- Published
- 2014-08
- Volume
- 24
- Issue
- 8
- Pages
- 464-471
- ISSN
- 0962-8924 (ISSN-L)
- PMC
- PMC4112140
- OpenAlex
- W1989674299
- Cited by
- 1,481
- References
- 71
- Citations by year
- 2026: 210 · 2025: 157 · 2024: 134 · 2023: 138 · 2022: 147 · 2021: 118 · 2020: 140 · 2019: 90 · 2018: 112 · 2017: 105 · 2016: 62 · 2015: 59 · 2014: 8
- FWCI
- 6.51
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Trends in Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- DSpace@MIT (Massachusetts Institute of Technology) (submittedVersion, cc-by-nc-nd)
- PMC
- Funders
- Glenn Foundation for Medical Research
- National Institutes of Health
- National Institute on Aging (R01AG024150, AG037457, R01AG037457, R01AG015339, AG024150, R01AG011119)
- Topics
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Aging › Genetics, Aging, and Longevity in Model Organisms
- Keywords
- NAD+, sirtuins, aging, NAD biosynthesis, visfatin, SIRT1, poly(ADP-ribose) polymerase, NAD+ precursors, anti-aging interventions, neurodegenerative diseases, mitochondrial function, circadian rhythm, metabolism
- MeSH terms
- Aging, Animals, Circadian Rhythm, Disease, Humans, Mitochondria, NAD, Sirtuins
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