NAD and the aging process: role in life, death and everything in between

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., Kalra, A., Prabhu, V. V., Allard, J. S., Lopez-Lluch, G., Lewis, K., et al. (2006) · Nature · doi:10.1038/nature05354 · Cited by 4,290 · see citing works

Chronic Inflammation (Inflammaging) and Its Potential Contribution to Age-Associated Diseases

Franceschi, C., & Campisi, J. (2014) · The Journals of Gerontology Series A: Biological Sciences and Medical Sciences · doi:10.1093/gerona/glu057 · Cited by 3,891 · see citing works

AMPK regulates energy expenditure by modulating NAD+ metabolism and SIRT1 activity

Cantó, C., Gerhart-Hines, Z., Feige, J. N., Lagouge, M., Noriega, L., Milne, J. C., Elliott, P. J., Puigserver, P., & Auwerx, J. (2009) · Nature · doi:10.1038/nature07813 · Cited by 3,300 · see citing works

Requirement of NAD and <i>SIR2</i> for Life-Span Extension by Calorie Restriction in <i>Saccharomyces cerevisiae</i>

Lin, S.-J., Defossez, P.-A., & Guarente, L. (2000) · Science · doi:10.1126/science.289.5487.2126 · Cited by 1,775 · see citing works

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., Gagne, D. J., Jin, L., Boss, O., Perni, R. B., Vu, C. B., et al. (2007) · Nature · doi:10.1038/nature06261 · Cited by 1,707 · see citing works

NAD+ Metabolism and the Control of Energy Homeostasis: A Balancing Act between Mitochondria and the Nucleus

Cantó, C., Menzies, K. J., & Auwerx, J. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.05.023 · Cited by 1,648 · see citing works

Declining NAD+ Induces a Pseudohypoxic State Disrupting Nuclear-Mitochondrial Communication during Aging

Gomes, 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 · see citing works

NAD+ and sirtuins in aging and disease

Imai, S.-I., & Guarente, L. (2014) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.04.002 · Cited by 1,481 · see citing works

Nicotinamide Mononucleotide, a Key NAD+ Intermediate, Treats the Pathophysiology of Diet- and Age-Induced Diabetes in Mice

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 · see citing works

NAD ⁺ in aging, metabolism, and neurodegeneration

Verdin, E. (2015) · Science · doi:10.1126/science.aac4854 · Cited by 1,319 · see citing works

Metabolic control of muscle mitochondrial function and fatty acid oxidation through SIRT1/PGC‐1α

Gerhart‐Hines, Z., Rodgers, J. T., Bare, O., Lerin, C., Kim, S., Mostoslavsky, R., Alt, F. W., Wu, Z., & Puigserver, P. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601633 · Cited by 1,294 · see citing works

A role for the mitochondrial deacetylase Sirt3 in regulating energy homeostasis

Ahn, B.-H., Kim, H.-S., Song, S., Lee, I. H., Liu, J., Vassilopoulos, A., Deng, C.-X., & Finkel, T. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0803790105 · Cited by 1,291 · see citing works

NAD ⁺ repletion improves mitochondrial and stem cell function and enhances life span in mice

Zhang, H., Ryu, D., Wu, Y., Gariani, K., Wang, X., Luan, P., D’Amico, D., Ropelle, E. R., Lutolf, M. P., Aebersold, R., et al. (2016) · Science · doi:10.1126/science.aaf2693 · Cited by 1,255 · see citing works

The NAD+ Precursor Nicotinamide Riboside Enhances Oxidative Metabolism and Protects against High-Fat Diet-Induced Obesity

Cantó, C., Houtkooper, R. H., Pirinen, E., Youn, D. Y., Oosterveer, M. H., Cen, Y., Fernandez-Marcos, P. J., Yamamoto, H., Andreux, P. A., Cettour-Rose, P., et al. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.04.022 · Cited by 1,238 · see citing works

Mammalian Sir2 homolog SIRT3 regulates global mitochondrial lysine acetylation

Lombard, D. B., Alt, F. W., Cheng, H.-L., Bunkenborg, J., Streeper, R. S., Mostoslavsky, R., Kim, J., Yancopoulos, G., Valenzuela, D., Murphy, A., et al. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01636-07 · Cited by 1,216 · see citing works

The NAD+/Sirtuin Pathway Modulates Longevity through Activation of Mitochondrial UPR and FOXO Signaling

Mouchiroud, L., Houtkooper, R. H., Moullan, N., Katsyuba, E., Ryu, D., Cantó, C., Mottis, A., Jo, Y.-S., Viswanathan, M., Schoonjans, K., et al. (2013) · Cell · doi:10.1016/j.cell.2013.06.016 · Cited by 1,210 · see citing works

Circadian Control of the NAD ⁺ Salvage Pathway by CLOCK-SIRT1

Nakahata, Y., Sahar, S., Astarita, G., Kaluzova, M., & Sassone-Corsi, P. (2009) · Science · doi:10.1126/science.1170803 · Cited by 1,198 · see citing works

Sirt3 mediates reduction of oxidative damage and prevention of age-related hearing loss under caloric restriction

Someya, S., Yu, W., Hallows, W. C., Xu, J., Vann, J. M., Leeuwenburgh, C., Tanokura, M., Denu, J. M., & Prolla, T. A. (2010) · Cell · doi:10.1016/j.cell.2010.10.002 · Cited by 1,150 · see citing works

SIRT1 and other sirtuins in metabolism

Chang, H.-C., & Guarente, L. (2014) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2013.12.001 · Cited by 1,138 · see citing works

Circadian Clock Feedback Cycle Through NAMPT-Mediated NAD ⁺ Biosynthesis

Ramsey, K. M., Yoshino, J., Brace, C. S., Abrassart, D., Kobayashi, Y., Marcheva, B., Hong, H.-K., Chong, J. L., Buhr, E. D., Lee, C., et al. (2009) · Science · doi:10.1126/science.1171641 · Cited by 1,126 · see citing works

Targeting CD38 with Daratumumab Monotherapy in Multiple Myeloma

Lokhorst, H. M., Plesner, T., Laubach, J. P., Nahi, H., Gimsing, P., Hansson, M., Minnema, M. C., Lassen, U., Krejcik, J., Palumbo, A., et al. (2015) · New England Journal of Medicine · doi:10.1056/nejmoa1506348 · Cited by 1,117 · see citing works

The sirtuin SIRT6 regulates lifespan in male mice

Kanfi, Y., Naiman, S., Amir, G., Peshti, V., Zinman, G., Nahum, L., Bar-Joseph, Z., & Cohen, H. Y. (2012) · Nature · doi:10.1038/nature10815 · Cited by 1,059 · see citing works

Inhibition of Silencing and Accelerated Aging by Nicotinamide, a Putative Negative Regulator of Yeast Sir2 and Human SIRT1

Bitterman, K. J., Anderson, R. M., Cohen, H. Y., Latorre-Esteves, M., & Sinclair, D. A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m205670200 · Cited by 1,002 · see citing works

Nutrient-Sensitive Mitochondrial NAD+ Levels Dictate Cell Survival

Yang, H., Yang, T., Baur, J. A., Perez, E., Matsui, T., Carmona, J. J., Lamming, D. W., Souza-Pinto, N. C., Bohr, V. A., Rosenzweig, A., et al. (2007) · Cell · doi:10.1016/j.cell.2007.07.035 · Cited by 950 · see citing works

Sirt1 protects against high-fat diet-induced metabolic damage

Pfluger, P. T., Herranz, D., Velasco-Miguel, S., Serrano, M., & Tschöp, M. H. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0802917105 · Cited by 928 · see citing works

Interdependence of AMPK and SIRT1 for metabolic adaptation to fasting and exercise in skeletal muscle

Cantó, C., Jiang, L. Q., Deshmukh, A. S., Mataki, C., Coste, A., Lagouge, M., Zierath, J. R., & Auwerx, J. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.02.006 · Cited by 921 · see citing works

CD38 Dictates Age-Related NAD Decline and Mitochondrial Dysfunction through an SIRT3-Dependent Mechanism

Camacho-Pereira, J., Tarragó, M. G., Chini, C. C. S., Nin, V., Escande, C., Warner, G. M., Puranik, A. S., Schoon, R. A., Reid, J. M., Galina, A., et al. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.05.006 · Cited by 901 · see citing works

The secret life of NAD+: an old metabolite controlling new metabolic signaling pathways

Houtkooper, R. H., Cantó, C., Wanders, R. J., & Auwerx, J. (2010) · Endocrine Reviews · doi:10.1210/er.2009-0026 · Cited by 899 · see citing works

Evolution and function of the ADP ribosyl cyclase/CD38 gene family in physiology and pathology

Malavasi, F., Deaglio, S., Funaro, A., Ferrero, E., Horenstein, A. L., Ortolan, E., Vaisitti, T., & Aydin, S. (2008) · Physiological Reviews · doi:10.1152/physrev.00035.2007 · Cited by 862 · see citing works

PARP-1 inhibition increases mitochondrial metabolism through SIRT1 activation

Bai, P., Cantó, C., Oudart, H., Brunyánszki, A., Cen, Y., Thomas, C., Yamamoto, H., Huber, A., Kiss, B., Houtkooper, R. H., et al. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.03.004 · Cited by 837 · see citing works

Glucose Restriction Inhibits Skeletal Myoblast Differentiation by Activating SIRT1 through AMPK-Mediated Regulation of Nampt

Fulco, M., Cen, Y., Zhao, P., Hoffman, E. P., McBurney, M. W., Sauve, A. A., & Sartorelli, V. (2008) · Developmental Cell · doi:10.1016/j.devcel.2008.02.004 · Cited by 821 · see citing works

Discoveries of Nicotinamide Riboside as a Nutrient and Conserved NRK Genes Establish a Preiss-Handler Independent Route to NAD+ in Fungi and Humans

Bieganowski, P., & Brenner, C. (2004) · Cell · doi:10.1016/s0092-8674(04)00416-7 · Cited by 750 · see citing works

Nicotinamide and PNC1 govern lifespan extension by calorie restriction in Saccharomyces cerevisiae

Anderson, R. M., Bitterman, K. J., Wood, J. G., Medvedik, O., & Sinclair, D. A. (2003) · Nature · doi:10.1038/nature01578 · Cited by 736 · see citing works

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., Milne, J. C., Lambert, P. D., Mataki, C., Elliott, P. J., & Auwerx, J. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.08.017 · Cited by 719 · see citing works

Physiological and pathophysiological roles of NAMPT and NAD metabolism.

Garten, A., Schuster, S., Penke, M., Gorski, T., de Giorgis, T., & Kiess, W. (2015) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2015.117 · Cited by 708 · see citing works

Nicotinic Acid, Nicotinamide, and Nicotinamide Riboside: A Molecular Evaluation of NAD ⁺ Precursor Vitamins in Human Nutrition

Bogan, K. L., & Brenner, C. (2008) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.28.061807.155443 · Cited by 707 · see citing works

Nicotinamide mononucleotide activation of a new DNA-dependent polyadenylic acid synthesizing nuclear enzyme

Chambon, P., Weill, J. D., & Mandel, P. (1963) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(63)90024-x · Cited by 654 · see citing works

SIRT2 deacetylates FOXO3a in response to oxidative stress and caloric restriction

Wang, F., Nguyen, M., Qin, F. X.-F., & Tong, Q. (2007) · Aging Cell · doi:10.1111/j.1474-9726.2007.00304.x · Cited by 652 · see citing works

SirT1 Gain of Function Increases Energy Efficiency and Prevents Diabetes in Mice

Banks, A. S., Kon, N., Knight, C. M., Matsumoto, M., Juárez, R. G., Rossetti, L., Gu, W. J., & Accili, D. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.08.014 · Cited by 636 · see citing works

Calorie restriction extends yeast life span by lowering the level of NADH

Lin, S.-J., Ford, E., Haigis, M., Liszt, G., & Guarente, L. (2004) · Genes &amp; Development · doi:10.1101/gad.1164804 · Cited by 632 · see citing works

SARM1 activation triggers axon degeneration locally via NAD ⁺ destruction

Gerdts, J., Brace, E. J., Sasaki, Y., DiAntonio, A., & Milbrandt, J. (2015) · Science · doi:10.1126/science.1258366 · Cited by 593 · see citing works

Interventions to slow aging in humans: are we ready?

Longo, V. D., Antebi, A., Bartke, A., Barzilai, N., Brown‐Borg, H. M., Caruso, C., Curiel, T. J., Cabo, R., Franceschi, C., Gems, D., et al. (2015) · Aging Cell · doi:10.1111/acel.12338 · Cited by 592 · see citing works

Pyridine nucleotide metabolites stimulate calcium release from sea urchin egg microsomes desensitized to inositol trisphosphate.

Clapper, D. L., Walseth, T. F., Dargie, P. J., & Lee, H. C. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47970-7 · Cited by 568 · see citing works

Regulation of the mPTP by SIRT3-mediated deacetylation of CypD at lysine 166 suppresses age-related cardiac hypertrophy

Hafner, A. V., Dai, J., Gomes, A. P., Xiao, C., Palmeira, C. M., Rosenzweig, A., & Sinclair, D. A. (2010) · Aging · doi:10.18632/aging.100252 · Cited by 547 · see citing works

Age-Associated Changes In Oxidative Stress and NAD+ Metabolism In Human Tissue

Massudi, H., Grant, R., Braidy, N., Guest, J., Farnsworth, B., & Guillemin, G. J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0042357 · Cited by 545 · see citing works

NAD + metabolism: Bioenergetics, signaling and manipulation for therapy

Yang, Y. J., & Sauve, A. A. (2016) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2016.06.014 · Cited by 488 · see citing works

Diet and exercise signals regulate SIRT3 and activate AMPK and PGC-1α in skeletal muscle

Palacios, O. M., Carmona, J. J., Michan, S., Chen, K. Y., Manabe, Y., III, J. L. W., Goodyear, L. J., & Tong, Q. (2009) · Aging · doi:10.18632/aging.100075 · Cited by 487 · see citing works

Nicotinamide N-methyltransferase knockdown protects against diet-induced obesity

Kraus, D., Yang, Q., Kong, D., Banks, A. S., Zhang, L., Rodgers, J. T., Pirinen, E., Pulinilkunnil, T., Gong, F., Wang, Y.-C., et al. (2014) · Nature · doi:10.1038/nature13198 · Cited by 487 · see citing works

In vivo NAD assay reveals the intracellular NAD contents and redox state in healthy human brain and their age dependences

Zhu, X.-H., Lu, M., Lee, B.-Y., Ugurbil, K., & Chen, W. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1417921112 · Cited by 468 · see citing works

Mechanism of Sirtuin Inhibition by Nicotinamide: Altering the NAD+ Cosubstrate Specificity of a Sir2 Enzyme

Avalos‬, J. L., Bever, K. M., & Wolberger, C. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.02.022 · Cited by 462 · see citing works

Effects of Sex, Strain, and Energy Intake on Hallmarks of Aging in Mice

Mitchell, S. J., Madrigal-Matute, J., Scheibye-Knudsen, M., Fang, E., Aon, M., González-Reyes, J. A., Cortassa, S., Kaushik, S., Gonzalez-Freire, M., Patel, B., et al. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.05.027 · Cited by 451 · see citing works

Cyclic ADP-ribose production by CD38 regulates intracellular calcium release, extracellular calcium influx and chemotaxis in neutrophils and is required for bacterial clearance in vivo

Partida-Sánchez, S., Cockayne, D. A., Monard, S., Jacobson, E. L., Oppenheimer, N., Garvy, B., Kusser, K., Goodrich, S., Howard, M., Harmsen, A., et al. (2001) · Nature Medicine · doi:10.1038/nm1101-1209 · Cited by 450 · see citing works

SirT1 Regulates Energy Metabolism and Response to Caloric Restriction in Mice

Boily, G., Seifert, E. L., Bevilacqua, L., He, X. H., Sabourin, G., Estey, C., Moffat, C., Crawford, S., Saliba, S., Jardine, K., et al. (2008) · PLoS ONE · doi:10.1371/journal.pone.0001759 · Cited by 444 · see citing works

SIRT3 Reverses Aging-Associated Degeneration

Brown, K., Xie, S., Qiu, X., Mohrin, M., Shin, J., Liu, Y., Zhang, D., Scadden, D. T., & Chen, D. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.01.005 · Cited by 436 · see citing works

Increase in Activity During Calorie Restriction Requires Sirt1

Chen, D., Steele, A. D., Lindquist, S., & Guarente, L. (2005) · Science · doi:10.1126/science.1118357 · Cited by 419 · see citing works

Biosensor reveals multiple sources for mitochondrial NAD ⁺

Cambronne, X. A., Stewart, M. L., Kim, D., Jones-Brunette, A. M., Morgan, R. K., Farrens, D. L., Cohen, M. S., & Goodman, R. H. (2016) · Science · doi:10.1126/science.aad5168 · Cited by 407 · see citing works

Nicotinamide mononucleotide supplementation reverses vascular dysfunction and oxidative stress with aging in mice

Picciotto, N. E., Gano, L. B., Johnson, L. C., Martens, C. R., Sindler, A. L., Mills, K. F., Imai, S., & Seals, D. R. (2016) · Aging Cell · doi:10.1111/acel.12461 · Cited by 396 · see citing works

Ten years of NAD-dependent SIR2 family deacetylases: implications for metabolic diseases

Imai, S., & Guarente, L. (2010) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2010.02.003 · Cited by 387 · see citing works

Eliciting the mitochondrial unfolded protein response by nicotinamide adenine dinucleotide repletion reverses fatty liver disease in mice

Gariani, K., Menzies, K. J., Ryu, D., Wegner, C. J., Wang, X., Ropelle, E. R., Moullan, N., Zhang, H., Perino, A., Lemos, V., et al. (2016) · Hepatology · doi:10.1002/hep.28245 · Cited by 368 · see citing works

Loss of NAD Homeostasis Leads to Progressive and Reversible Degeneration of Skeletal Muscle

Frederick, D. W., Loro, E., Liu, L., Davila, A., Chellappa, K., Silverman, I. M., Quinn, W. J., Gosai, S. J., Tichy, E. D., Davis, J. G., et al. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.07.005 · Cited by 367 · see citing works

mTOR Regulates Lysosomal ATP-Sensitive Two-Pore Na+ Channels to Adapt to Metabolic State

Cang, C., Zhou, Y., Navarro, B., Seo, Y.-J., Aranda, K., Shi, L. L., Battaglia-Hsu, S.-F., Nissim, I., Clapham, D. E., & Ren, D. (2013) · Cell · doi:10.1016/j.cell.2013.01.023 · Cited by 361 · see citing works

ADP-ribosyl cyclase: an enzyme that cyclizes NAD+ into a calcium-mobilizing metabolite.

Lee, H. C., & Aarhus, R. (1991) · Cell Regulation · doi:10.1091/mbc.2.3.203 · Cited by 355 · see citing works

Regulation of intracellular levels of NAD: A novel role for CD38

Aksoy, P., White, T. A., Thompson, M., & Chini, E. N. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.05.042 · Cited by 353 · see citing works

Monoclonal antibodies targeting <scp>CD</scp>38 in hematological malignancies and beyond

van de Donk, N. W. C. J., Janmaat, M. L., Mutis, T., Lammerts van Bueren, J. J., Ahmadi, T., Sasser, A. K., Lokhorst, H. M., & Parren, P. W. H. I. (2016) · Immunological Reviews · doi:10.1111/imr.12389 · Cited by 353 · see citing works

A high-fat diet and NAD(+) activate Sirt1 to rescue premature aging in Cockayne syndrome

Scheibye-Knudsen, M., Mitchell, S. J., Fang, E. F., Iyama, T., Ward, T., Wang, J., Dunn, C. A., Singh, N., Veith, S., Hasan-Olive, M. M., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.10.005 · Cited by 352 · see citing works

NAD+-Dependent Activation of Sirt1 Corrects the Phenotype in a Mouse Model of Mitochondrial Disease

Cerutti, R., Pirinen, E., Lamperti, C., Marchet, S., Sauve, A. A., Li, W., Leoni, V., Schon, E. A., Dantzer, F., Auwerx, J., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.04.001 · Cited by 343 · see citing works

Flavonoid Apigenin Is an Inhibitor of the NAD+ase CD38

Escande, C., Nin, V., Price, N. L., Capellini, V., Gomes, A. P., Barbosa, M. T., O’Neil, L., White, T. A., Sinclair, D. A., & Chini, E. N. (2013) · Diabetes · doi:10.2337/db12-1139 · Cited by 332 · see citing works

Extension of Human Cell Lifespan by Nicotinamide Phosphoribosyltransferase

van der Veer, E., Ho, C. S. W., O’Neil, C. H., Barbosa, N., Scott, R., Cregan, S. P., & Pickering, J. G. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.c700018200 · Cited by 325 · see citing works

Age‐associated loss of Sirt1‐mediated enhancement of glucose‐stimulated insulin secretion in beta cell‐specific Sirt1‐overexpressing (BESTO) mice

Ramsey, K. M., Mills, K. F., Satoh, A., & Imai, S. (2008) · Aging Cell · doi:10.1111/j.1474-9726.2007.00355.x · Cited by 321 · see citing works

Forever young: SIRT3 a shield against mitochondrial meltdown, aging, and neurodegeneration

Kincaid, B., & Bossy‐Wetzel, E. (2013) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2013.00048 · Cited by 314 · see citing works

Poly(ADP-ribose) polymerase activity in mononuclear leukocytes of 13 mammalian species correlates with species-specific life span.

Grube, K., & Bürkle, A. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.24.11759 · Cited by 301 · see citing works

Regulation of SIRT1 in aging: Roles in mitochondrial function and biogenesis

Yuan, Y., Cruzat, V. F., Newsholme, P., Cheng, J., Chen, Y., & Lu, Y. (2016) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2016.02.003 · Cited by 301 · see citing works

Nicotinamide Riboside Opposes Type 2 Diabetes and Neuropathy in Mice

Trammell, S. A. J., Weidemann, B. J., Chadda, A., Yorek, M. S., Holmes, A., Coppey, L. J., Obrosov, A., Kardon, R. H., Yorek, M. A., & Brenner, C. (2016) · Scientific Reports · doi:10.1038/srep26933 · Cited by 301 · see citing works

SRT1720 improves survival and healthspan of obese mice

Minor, R. K., Baur, J. A., Gomes, A. P., Ward, T. M., Csiszár, A., Mercken, E. M., Abdelmohsen, K., Shin, Y., Cantó, C., Scheibye‐Knudsen, M., et al. (2011) · Scientific Reports · doi:10.1038/srep00070 · Cited by 297 · see citing works

Skeletal muscle NAMPT is induced by exercise in humans

Costford, S. R., Bajpeyi, S., Pasarica, M., Albarado, D. C., Thomas, S. C., Xie, H., Church, T. S., Jubrias, S. A., Conley, K. E., & Smith, S. R. (2009) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00318.2009 · Cited by 297 · see citing works

Exercise alters SIRT1, SIRT6, NAD and NAMPT levels in skeletal muscle of aged rats

Koltai, E., Szabo, Z., Atalay, M., Boldogh, I., Naito, H., Goto, S., Nyakas, C., & Radak, Z. (2010) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2009.11.002 · Cited by 283 · see citing works

SIRT1 Deficiency in Microglia Contributes to Cognitive Decline in Aging and Neurodegeneration via Epigenetic Regulation of IL-1β

Cho, S.-H., Chen, J. A., Sayed, F., Ward, M. E., Gao, F., Nguyen, T. A., Krabbe, G., Sohn, P. D., Lo, I., Minami, S., et al. (2015) · The Journal of Neuroscience · doi:10.1523/jneurosci.2939-14.2015 · Cited by 275 · see citing works

CD38 and CD157: A long journey from activation markers to multifunctional molecules

Quarona, V., Zaccarello, G., Chillemi, A., Brunetti, E., Singh, V. K., Ferrero, E., Funaro, A., Horenstein, A. L., & Malavasi, F. (2013) · Cytometry Part B Clinical Cytometry · doi:10.1002/cyto.b.21092 · Cited by 269 · see citing works

Specific ablation of Nampt in adult neural stem cells recapitulates their functional defects during aging

Stein, L. R., & Imai, S. (2014) · The EMBO Journal · doi:10.1002/embj.201386917 · Cited by 265 · see citing works

Pharmacological Inhibition of poly(ADP-ribose) polymerases improves fitness and mitochondrial function in skeletal muscle

Pirinen, E., Cantó, C., Jo, Y. S., Morato, L., Zhang, H., Menzies, K. J., Williams, E. G., Mouchiroud, L., Moullan, N., Hagberg, C., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.04.002 · Cited by 254 · see citing works

Synthesis and Degradation of Cyclic ADP-Ribose by NAD Glycohydrolases

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NAD metabolism: Role in senescence regulation and aging

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