Therapeutic Potential of NAD-Boosting Molecules: The In Vivo Evidence

Rajman, Luis; Chwalek, Karolina; Sinclair, David A.

doi:10.1016/j.cmet.2018.02.011

Cited by 865Sirtuins and Resveratrol in MedicineBiochemical and Molecular ResearchGenetics, Aging, and Longevity in Model Organisms

Therapeutic Potential of NAD-Boosting Molecules: The In Vivo Evidence

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Rajman, Luis, Chwalek, Karolina, Sinclair, David A.·2018·Cell Metabolism

DOI 10.1016/j.cmet.2018.02.011PMC PMC6342515

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Abstract

Nicotinamide adenine dinucleotide (NAD), the cell's hydrogen carrier for redox enzymes, is well known for its role in redox reactions. More recently, it has emerged as a signaling molecule. By modulating NAD+-sensing enzymes, NAD+ controls hundreds of key processes from energy metabolism to cell survival, rising and falling depending on food intake, exercise, and the time of day. NAD+ levels steadily decline with age, resulting in altered metabolism and increased disease susceptibility. Restoration of NAD+ levels in old or diseased animals can promote health and extend lifespan, prompting a search for safe and efficacious NAD-boosting molecules that hold the promise of increasing the body's resilience, not just to one disease, but to many, thereby extending healthy human lifespan.

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NAD+ or NAD precursors can increase healthspan in experimental animals.
“NAD+ or NAD precursors can increase healthspan in experimental animals141.”
From Cellular senescence and senolytics: the path to the clinic (2022) · cites this paper as [141]
NAD+ precursor administration is a simple and convenient strategy to activate NAD+ synthesis and increase NAD+ levels.
“NAD+ precursor administration is a simple and convenient strategy to activate NAD+ synthesis and increase NAD+ levels (9).”
From Nicotinamide riboside and nicotinamide mononucleotide facilitate NAD + synthesis via enterohepatic circulation (2025) · cites this paper as [9]
NR and NMN have a protective effect in a number of age-related disease models, by increasing the pool of precursors and thus NAD+ levels in the body.
“According to reports, NR and NMN have a protective effect in a number of age-related disease models, by increasing the pool of precursors and thus NAD+ levels in the body, both of which have been tested in murine and invertebrate aging studies [195, 197, 199].”
From Immunosenescence: a key player in cancer development (2020) · cites this paper as [195]
NAD+ declines in many tissues during the aging process, including adipose tissue, skeletal muscle, brain, liver, pancreas, heart, spleen, kidney, and lungs, leading to various age-related pathophysiology developments.
“Much of the literature suggests that NAD+ declines in many tissues during the aging process, including adipose tissue, skeletal muscle, brain, liver, pancreas, heart, spleen, kidney, and lungs, leading to various age-related pathophysiology developments [195–197].”
From Immunosenescence: a key player in cancer development (2020) · cites this paper as [195]
Systematic NAD+ decline and decreased sirtuin activity are considered molecular events of ageing that may underlie the increase in age-related diseases limiting lifespan.
“Systematic NAD+ decline and decreased sirtuin activity are considered among the molecular events that occur during ageing, possibly underlying the increase in age-related diseases that limit organismal lifespan251.”
From Mitochondrial and metabolic dysfunction in ageing and age-related diseases (2022) · cites this paper as [251]

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Mitochondrial Complex I Deficiency Increases Protein Acetylation and Accelerates Heart Failure
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In vivo NAD assay reveals the intracellular NAD contents and redox state in healthy human brain and their age dependences
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Biology of Poly(ADP-Ribose) Polymerases: The Factotums of Cell Maintenance
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NAD + Depletion Is Necessary and Sufficient forPoly(ADP-Ribose) Polymerase-1-Mediated Neuronal Death
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Mitochondrial complex I activity and NAD+/NADH balance regulate breast cancer progression
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Efficacy and safety of high-density lipoprotein cholesterol-increasing compounds
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Poly(ADP-Ribose) Regulates Stress Responses and MicroRNA Activity in the Cytoplasm
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Acetylation Regulates Gluconeogenesis by Promoting PEPCK1 Degradation via Recruiting the UBR5 Ubiquitin Ligase
Jiang, W., Wang, S., Xiao, M., Lin, Y., Zhou, L., Lei, Q., Xiong, Y., Guan, K., & Zhao, S. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.04.028 · Cited by 415 · see citing works
Nicotinamide Riboside Promotes Sir2 Silencing and Extends Lifespan via Nrk and Urh1/Pnp1/Meu1 Pathways to NAD+
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Biosensor reveals multiple sources for mitochondrial NAD +
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An ARC/Mediator subunit required for SREBP control of cholesterol and lipid homeostasis
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The 193-Kd Vault Protein, Vparp, Is a Novel Poly(Adp-Ribose) Polymerase
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Nicotinamide mononucleotide supplementation reverses vascular dysfunction and oxidative stress with aging in mice
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Poly(ADP-ribose) Polymerase-1-dependent Cardiac Myocyte Cell Death during Heart Failure Is Mediated by NAD+ Depletion and Reduced Sir2α Deacetylase Activity
Pillai, J. B., Isbatan, A., Imai, S., & Gupta, M. P. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506162200 · Cited by 391 · see citing works
Sirtuin 3-dependent mitochondrial dynamic improvements protect against acute kidney injury.
Morigi, M., Perico, L., Rota, C., Longaretti, L., Conti, S., Rottoli, D., Novelli, R., Remuzzi, G., & Benigni, A. (2015) · Journal of Clinical Investigation · doi:10.1172/jci77632 · Cited by 388 · see citing works
NRK1 controls nicotinamide mononucleotide and nicotinamide riboside metabolism in mammalian cells
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“In rodents, NR is more efficient in boosting NAD+ than NA and NAM (Trammell et al., 2016a), possibly due to increased uptake (Imai, 2009; Imai and Guarente, 2014; Ratajczak et al., 2016; Revollo et al., 2007a).”
Influential
Sarm1-Mediated Axon Degeneration Requires Both SAM and TIR Interactions
Gerdts, J., Summers, D. W., Sasaki, Y., DiAntonio, A., & Milbrandt, J. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.1197-13.2013 · Cited by 375 · see citing works
Eliciting the mitochondrial unfolded protein response by nicotinamide adenine dinucleotide repletion reverses fatty liver disease in mice
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Indoleamine 2,3‐dioxygenase contributes to tumor cell evasion of T cell‐mediated rejection
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Visfatin in overweight/obesity, type 2 diabetes mellitus, insulin resistance, metabolic syndrome and cardiovascular diseases: a meta‐analysis and systemic review
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Discovery of a Proneurogenic, Neuroprotective Chemical
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Nicotinamide riboside restores cognition through an upregulation of proliferator-activated receptor-γ coactivator 1α regulated β-secretase 1 degradation and mitochondrial gene expression in Alzheimer's mouse models
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NAD+-Dependent Activation of Sirt1 Corrects the Phenotype in a Mouse Model of Mitochondrial Disease
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“In 1963, a breakthrough camewith the discovery that NAD+ is a co-substrate for the addition of poly-ADP-ribose to proteins (Chambon et al., 1963).”
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
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Pathways and Subcellular Compartmentation of NAD Biosynthesis in Human Cells
Nikiforov, A., Dölle, C., Niere, M., & Ziegler, M. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.213298 · Cited by 326 · see citing works
PARP-3 and APLF Function Together to Accelerate Nonhomologous End-Joining
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The Role of PARP-1 and PARP-2 Enzymes in Metabolic Regulation and Disease
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The regulation of nicotinamide adenine dinucleotide biosynthesis by Nampt/PBEF/visfatin in mammals
Revollo, J. R., Grimm, A. A., & Imai, S. (2007) · Current Opinion in Gastroenterology · doi:10.1097/mog.0b013e32801b3c8f · Cited by 311 · see citing works
Nicotinamide Mononucleotide, an Intermediate of NAD+ Synthesis, Protects the Heart from Ischemia and Reperfusion
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Poly(ADP-ribose) polymerase activity in mononuclear leukocytes of 13 mammalian species correlates with species-specific life span.
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The Deacetylase Sirt6 Activates the Acetyltransferase GCN5 and Suppresses Hepatic Gluconeogenesis
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Manipulation of a Nuclear NAD+ Salvage Pathway Delays Aging without Altering Steady-state NAD+ Levels
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Partitioning Circadian Transcription by SIRT6 Leads to Segregated Control of Cellular Metabolism
Masri, S., Rigor, P., Cervantes, M., Ceglia, N., Sebastian, C., Xiao, C., Roqueta-Rivera, M., Deng, C., Osborne, T. F., Mostoslavsky, R., et al. (2014) · Cell · doi:10.1016/j.cell.2014.06.050 · Cited by 292 · see citing works
Enzymology of NAD+ homeostasis in man
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Nicotinamide Phosphoribosyltransferase Regulates Cell Survival Through NAD + Synthesis in Cardiac Myocytes
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PARP9 and PARP14 cross-regulate macrophage activation via STAT1 ADP-ribosylation
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Activation of SIRT3 by the NAD(+) precursor nicotinamide riboside protects from noise-induced hearing loss
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Tankyrase Is a Golgi-associated Mitogen-activated Protein Kinase Substrate That Interacts with IRAP in GLUT4 Vesicles
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Lethal Cardiomyopathy in Mice Lacking Transferrin Receptor in the Heart
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CD38 and CD157: A long journey from activation markers to multifunctional molecules
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An open-label, non-randomized study of the pharmacokinetics of the nutritional supplement nicotinamide riboside (NR) and its effects on blood NAD+ levels in healthy volunteers
Airhart, S. E., Shireman, L. M., Risler, L. J., Anderson, G. D., Gowda, G. A. N., Raftery, D., Tian, R., Shen, D. D., & O’Brien, K. D. (2017) · PLoS ONE · doi:10.1371/journal.pone.0186459 · Cited by 260 · see citing works
Tankyrase-1 polymerization of poly(ADP-ribose) is required for spindle structure and function
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NAD + repletion improves muscle function in muscular dystrophy and counters global PARylation
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Pharmacological Inhibition of poly(ADP-ribose) polymerases improves fitness and mitochondrial function in skeletal muscle
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The enzyme CD38 (a NAD glycohydrolase, EC 3.2.2.5) is necessary for the development of diet‐induced obesity
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Nicotinic Acid Limitation Regulates Silencing of Candida Adhesins During UTI
Domergue, R., Castaño, I., De Las Peñas, A., Zupancic, M., Lockatell, V., Hebel, J. R., Johnson, D., & Cormack, B. P. (2005) · Science · doi:10.1126/science.1108640 · Cited by 249 · see citing works
A rise in NAD precursor nicotinamide mononucleotide (NMN) after injury promotes axon degeneration
Di Stefano, M., Nascimento-Ferreira, I., Orsomando, G., Mori, V, Gilley, J., Brown, R., Janeckova, L., Vargas, M. E., Worrell, L. A., Loreto, A., et al. (2015) · Cell Death & Differentiation · doi:10.1038/cdd.2014.164 · Cited by 246 · cited 1× · see citing works
“There is some evidence indicating that NMN treatment promotes axon degeneration and that the dependence on NMNAT2 for axon survival is due to its consumption of NMN rather than its NAD synthesis activity (Di Stefano et al., 2015).”
SIRT2 induces the checkpoint kinase BubR1 to increase lifespan
North, B. J., Rosenberg, M. A., Jeganathan, K. B., Hafner, A. V., Michán, S., Dai, J., Baker, D. J., Cen, Y., Wu, L. E., Sauve, A. A., et al. (2014) · The EMBO Journal · doi:10.15252/embj.201386907 · Cited by 244 · see citing works
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P7C3 Neuroprotective Chemicals Function by Activating the Rate-Limiting Enzyme in NAD Salvage
Wang, G., Han, T., Nijhawan, D., Theodoropoulos, P., Naidoo, J., Yadavalli, S., Mirzaei, H., Pieper, A. A., Ready, J. M., & McKnight, S. L. (2014) · Cell · doi:10.1016/j.cell.2014.07.040 · Cited by 243 · see citing works
Nicotinamide Mononucleotide, an NAD+ Precursor, Rescues Age-Associated Susceptibility to AKI in a Sirtuin 1–Dependent Manner
Guan, Y., Wang, S.-R., Huang, X.-Z., Xie, Q.-H., Xu, Y.-Y., Shang, D., & Hao, C.-M. (2017) · Journal of the American Society of Nephrology · doi:10.1681/asn.2016040385 · Cited by 238 · see citing works
Enzymology of Nad + Synthesis
Magni, G., Amici, A., Emanuelli, M., Raffaelli, N., & Ruggieri, S. (1999) · Advances in enzymology and related areas of molecular biology/Advances in enzymology and related subjects · doi:10.1002/9780470123195.ch5 · Cited by 235 · see citing works
Nicotinamide Phosphoribosyltransferase (Nampt): A Link Between NAD Biology, Metabolism, and Diseases
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The importance of NAMPT / NAD / SIRT1 in the systemic regulation of metabolism and ageing
Imai, S., & Yoshino, J. (2013) · Diabetes Obesity and Metabolism · doi:10.1111/dom.12171 · Cited by 232 · see citing works
Identification of a New Urate and High Affinity Nicotinate Transporter, hOAT10 (SLC22A13)
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Tumor suppressor p53 cooperates with SIRT6 to regulate gluconeogenesis by promoting FoxO1 nuclear exclusion
Zhang, P., Tu, B., Wang, H., Cao, Z., Tang, M., Zhang, C., Gu, B., Li, Z., Wang, L., Yang, Y., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1411026111 · Cited by 222 · see citing works
Evidence that vault ribonucleoprotein particles localize to the nuclear pore complex
Chugani, D. C., Rome, L. H., & Kedersha, N. (1993) · Journal of Cell Science · doi:10.1242/jcs.106.1.23 · Cited by 219 · see citing works
Nicotinamide mononucleotide protects against β-amyloid oligomer-induced cognitive impairment and neuronal death
Wang, X., Hu, X., Yang, Y., Takata, T., & Sakurai, T. (2016) · Brain Research · doi:10.1016/j.brainres.2016.04.060 · Cited by 217 · see citing works
Effects of the pure flavonoids epicatechin and quercetin on vascular function and cardiometabolic health: a randomized, double-blind, placebo-controlled, crossover trial
Dower, J. I., Geleijnse, J. M., Gijsbers, L., Zock, P. L., Kromhout, D., & Hollman, P. C. H. (2015) · American Journal of Clinical Nutrition · doi:10.3945/ajcn.114.098590 · Cited by 216 · see citing works
Mitochondrial protein hyperacetylation in the failing heart
Horton, J. L., Martin, O. J., Lai, L., Riley, N. M., Richards, A., Vega, R. B., Leone, T. C., Pagliarini, D. J., Muoio, D. M., Bedi, K. C., et al. (2016) · JCI Insight · doi:10.1172/jci.insight.84897 · Cited by 208 · see citing works
Inhibition of De Novo NAD + Synthesis by Oncogenic URI Causes Liver Tumorigenesis through DNA Damage
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Elevation of cellular NAD levels by nicotinic acid and involvement of nicotinic acid phosphoribosyltransferase in human cells
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Extracellular nicotinamide phosphoribosyltransferase (NAMPT) promotes M2 macrophage polarization in chronic lymphocytic leukemia
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Children with autism spectrum disorders, who improved with a luteolin-containing dietary formulation, show reduced serum levels of TNF and IL-6
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Leucocytes are a major source of circulating nicotinamide phosphoribosyltransferase (NAMPT)/pre-B cell colony (PBEF)/visfatin linking obesity and inflammation in humans
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Effect of nicotinamide mononucleotide on brain mitochondrial respiratory deficits in an Alzheimer’s disease-relevant murine model
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Hepatic NAD+ deficiency as a therapeutic target for non‐alcoholic fatty liver disease in ageing
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Dietary niacin and the risk of incident Alzheimer’s disease and of cognitive decline
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Absence of SARM1 Rescues Development and Survival of NMNAT2-Deficient Axons
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UV Radiation-Induced Immunosuppression Is Greater in Men and Prevented by Topical Nicotinamide
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Diet and Parkinson's disease II
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NMNAT1 inhibits axon degeneration via blockade of SARM1-mediated NAD+ depletion
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PARP16 is a tail-anchored endoplasmic reticulum protein required for the PERK- and IRE1α-mediated unfolded protein response
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Apigenin inhibits prostate cancer progression in TRAMP mice via targeting PI3K/Akt/FoxO pathway
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An 85-kb tandem triplication in the slow Wallerian degeneration ( Wld s ) mouse
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A conserved NAD + binding pocket that regulates protein-protein interactions during aging
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Self-citation
CardioPulse
Nichols, M. S., Townsend, N. P., Scarborough, P., et al. (2014) · European Heart Journal · doi:10.1093/eurheartj/ehu378 · Cited by 186 · see citing works
Tankyrases: Structure, Function and Therapeutic Implications in Cancer
Haikarainen, T., Krauss, S. J. K., & Lehtiö, L. (2014) · Current Pharmaceutical Design · doi:10.2174/1381612820666140630101525 · Cited by 185 · see citing works
NAMPT-Mediated NAD+ Biosynthesis Is Essential for Vision In Mice
Lin, J. B., Kubota, S., Ban, N., Yoshida, M., Santeford, A. C., Sène, A., Nakamura, R. E. I., Zapata, N., Kubota, M., Tsubota, K., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.08.073 · Cited by 185 · see citing works
Effect of quercetin on traits of the metabolic syndrome, endothelial function and inflammation in men with different APOE isoforms
Pfeuffer, M., Auinger, A., Bley, U., Kraus-Stojanowic, I., Laue, C., Winkler, P., Rüfer, C. E., Frank, J., Boesch‐Saadatmandi, C., Rimbach, G. H., et al. (2011) · Nutrition Metabolism and Cardiovascular Diseases · doi:10.1016/j.numecd.2011.08.010 · Cited by 182 · see citing works
Expression and regulation of Runx2/Cbfa1 and osteoblast phenotypic markers during the growth and differentiation of human osteoblasts
Prince, M., Banerjee, C., Javed, A., Green, J., Lian, J. B., Stein, G. S., Bodine, P. V. N., & Komm, B. S. (2000) · Journal of Cellular Biochemistry · doi:10.1002/1097-4644(20010301)80:3 · Cited by 182 · see citing works
Hallucinations, sleep fragmentation, and altered dream phenomena in Parkinson's disease
Pappert, E. J., Goetz, C. G., Niederman, F. G., Raman, R., & Leurgans, S. E. (1999) · Movement Disorders · doi:10.1002/1531-8257(199901)14:1 · Cited by 180 · see citing works
Rapid Evolution of PARP Genes Suggests a Broad Role for ADP-Ribosylation in Host-Virus Conflicts
Daugherty, M. D., Young, J. M., Kerns, J. A., & Malik, H. S. (2014) · PLoS Genetics · doi:10.1371/journal.pgen.1004403 · Cited by 176 · see citing works
Dietary Flavones and Flavonoles Are Inhibitors of Poly(ADP-ribose)polymerase-1 in Pulmonary Epithelial Cells ,
Geraets, L., Moonen, H. J. J., Brauers, K. J. J., Wouters, E. F. �., Bast, A., & Hageman, G. J. (2007) · Journal of Nutrition · doi:10.1093/jn/137.10.2190 · Cited by 175 · see citing works
Life Span Extension and Neuronal Cell Protection by Drosophila Nicotinamidase
Balan, V., Miller, G. S., Kaplun, L., Balan, K., Chong, Z.-Z., Li, F., Kaplun, A., VanBerkum, M. F. A., Arking, R., Freeman, D. C., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m804681200 · Cited by 174 · see citing works
Regulation of SIRT 1 mediated NAD dependent deacetylation: A novel role for the multifunctional enzyme CD38
Aksoy, P., Escande, C., White, T. A., Thompson, M., Soares, S. M., Benech, J. C., & Chini, E. N. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.08.066 · Cited by 173 · see citing works
Increased neopterin production and tryptophan degradation in advanced Parkinson's disease.
Widner, B., Leblhuber, F., & Fuchs, D. (2002) · Journal of Neural Transmission · doi:10.1007/s007020200014 · Cited by 171 · see citing works
Inhibiting poly ADP-ribosylation increases fatty acid oxidation and protects against fatty liver disease
Gariani, K., Ryu, D., Menzies, K. J., Yi, H.-S., Stein, S., Zhang, H., Perino, A., Lemos, V., Katsyuba, E., Jha, P., et al. (2017) · Journal of Hepatology · doi:10.1016/j.jhep.2016.08.024 · Cited by 167 · cited 17× · see citing works
“The majority of NAD+ is salvaged from NAM, the product of CD38 and the PARPs (Magni et al., 1999, 2004) or from the various forms of niacin taken up in the diet, including NAM, NA, nicotinamide riboside (NR), and nicotinamide mononucleotide (NMN) (Bogan and Brenner, 2008; Mills et al., 2016; Trammell et al., 2016b; Um…”
Influential
Regulation of NF-κB signalling by the mono-ADP-ribosyltransferase ARTD10
Verheugd, P., Forst, A. H., Milke, L., Herzog, N., Feijs, K. L. H., Kremmer, E., Kleine, H. O., & Lüscher, B. (2013) · Nature Communications · doi:10.1038/ncomms2672 · Cited by 160 · see citing works
Molecular Characteristics of Serum Visfatin and Differential Detection by Immunoassays
Körner, A., Garten, A., Blüher, M., Tauscher, R., Kratzsch, J., & Kieß, W. (2007) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2007-1304 · Cited by 159 · see citing works
Protecting Axonal Degeneration by Increasing Nicotinamide Adenine Dinucleotide Levels in Experimental Autoimmune Encephalomyelitis Models
Kaneko, S., Wang, J., Kaneko, M., Yiu, G. C., Hurrell, J., Chitnis, T., Khoury, S. J., & He, Z. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.2116-06.2006 · Cited by 159 · see citing works
CD73 Protein as a Source of Extracellular Precursors for Sustained NAD+ Biosynthesis in FK866-treated Tumor Cells
Grozio, A., Sociali, G., Sturla, L., Caffa, I., Soncini, D., Salis, A., Raffaelli, N., De Flora, A., Nencioni, A., & Bruzzone, S. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.470435 · Cited by 158 · cited 4× · see citing works
“Extracellularly, NAD+ is cleaved to NMN and AMP by nucleotide pyrophosphatases including CD73 (Aleo et al., 2001; Grozio et al., 2013), while the transmembrane glycohydrolases CD38 and CD157 cleave NAD+ to generate NAM and ADPR and can also act as ADP-ribosyl cyclases that catalyze the hydrolysis of NAD+ to generate N…”
Influential
Metabolic Profiling of Alternative NAD Biosynthetic Routes in Mouse Tissues
Mori, V., Amici, A., Mazzola, F., Stefano, M. D., Conforti, L., Magni, G., Ruggieri, S., Raffaelli, N., & Orsomando, G. (2014) · PLoS ONE · doi:10.1371/journal.pone.0113939 · Cited by 158 · see citing works
A review of nicotinamide: treatment of skin diseases and potential side effects
Rolfe, H. M. (2014) · Journal of Cosmetic Dermatology · doi:10.1111/jocd.12119 · Cited by 158 · see citing works
Targeting of NAD Metabolism in Pancreatic Cancer Cells: Potential Novel Therapy for Pancreatic Tumors
Chini, C. C. S., Guerrico, A. M. G., Nin, V., Camacho-Pereira, J., Escande, C., Barbosa, M. T., & Chini, E. N. (2013) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-13-0150 · Cited by 147 · see citing works
PARP inhibitors: the race is on
Brown, J. S., Kaye, S. B., & Yap, T. A. (2016) · British Journal of Cancer · doi:10.1038/bjc.2016.67 · Cited by 147 · see citing works
Discovery, synthesis, and biological evaluation of thiazoloquin(az)olin(on)es as potent CD38 inhibitors
Haffner, C. D., Becherer, J. D., Boros, E. E., Cadilla, R., Carpenter, T., Cowan, D., Deaton, D. N., Guo, Y., Harrington, W., Henke, B. R., et al. (2015) · Journal of Medicinal Chemistry · doi:10.1021/jm502009h · Cited by 137 · see citing works
SARM1-specific motifs in the TIR domain enable NAD + loss and regulate injury-induced SARM1 activation
Summers, D. W., Gibson, D. A., DiAntonio, A., & Milbrandt, J. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1601506113 · Cited by 135 · see citing works
Oral nicotinamide protects against ultraviolet radiation-induced immunosuppression in humans
Yiasemides, E., Sivapirabu, G., Halliday, G. M., Park, J., & Damian, D. L. (2008) · Carcinogenesis · doi:10.1093/carcin/bgn248 · Cited by 134 · see citing works
Impact of Flavonols on Cardiometabolic Biomarkers: A Meta‐Analysis of Randomized Controlled Human Trials to Explore the Role of Inter‐Individual Variability
Menezes, R., Rodriguez‐Mateos, A., Καλτσάτου, Α., González‐Sarrías, A., Greyling, A., Giannaki, C. D., Andrés‐Lacueva, C., Milenković, D., Gibney, E. R., Dumont, J., et al. (2017) · Nutrients · doi:10.3390/nu9020117 · Cited by 132 · see citing works
Neuroprotective efficacy of aminopropyl carbazoles in a mouse model of Parkinson disease
Jesús‐Cortés, H. D., Xu, P., Drawbridge, J., Estill, S. J., Huntington, P. J., Tran, S., Britt, J. K., Tesla, R., Morlock, L., Naidoo, J., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1213956109 · Cited by 130 · see citing works
Sirtuin 1 Regulates Hepatitis B Virus Transcription and Replication by Targeting Transcription Factor AP-1
Ren, J., Tao, Y., Zhang, Z., Chen, W., Cai, X.-F., Chen, K., Ko, B. C. B., Song, C., Ran, L.-K., Li, W., et al. (2013) · Journal of Virology · doi:10.1128/jvi.02861-13 · Cited by 130 · see citing works
Neuroprotective efficacy of aminopropyl carbazoles in a mouse model of amyotrophic lateral sclerosis
Tesla, R., Wolf, H. P., Xu, P., Drawbridge, J., Estill, S. J., Huntington, P., McDaniel, L., Knobbe, W., Burket, A., Tran, S., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1213960109 · Cited by 129 · see citing works
Nicotinamide mononucleotide requires SIRT3 to improve cardiac function and bioenergetics in a Friedreich’s ataxia cardiomyopathy model
Martin, A. S., Abraham, D. M., Hershberger, K. A., Bhatt, D. P., Mao, L., Cui, H., Liu, J., Liu, X., Muehlbauer, M. J., Grimsrud, P. A., et al. (2017) · JCI Insight · doi:10.1172/jci.insight.93885 · Cited by 128 · see citing works
Apollo-NADP+: a spectrally tunable family of genetically encoded sensors for NADP+
Cameron, D. W., Bui, C. V., Hutchinson, A., Loppnau, P., Gräslund, S., & Rocheleau, J. V. (2016) · Nature Methods · doi:10.1038/nmeth.3764 · Cited by 126 · see citing works
Nicotinamide mononucleotide attenuates brain injury after intracerebral hemorrhage by activating Nrf2/HO-1 signaling pathway
Wei, C., Kong, Y., Li, G., Guan, Y., Wang, P., & Miao, C. (2017) · Scientific Reports · doi:10.1038/s41598-017-00851-z · Cited by 126 · see citing works
A cellular survival switch: poly(ADP‐ribosyl)ation stimulates DNA repair and silences transcription
Ziegler, M., & Oei, S. L. (2001) · BioEssays · doi:10.1002/bies.1074 · Cited by 125 · see citing works
P7C3 Neuroprotective Chemicals Block Axonal Degeneration and Preserve Function after Traumatic Brain Injury
Yin, T. C., Britt, J. K., Jesús‐Cortés, H. D., Lü, Y., Genova, R. M., Khan, M. Z., Voorhees, J. R., Shao, J., Katzman, A. C., Huntington, P. J., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.08.030 · Cited by 123 · see citing works
Nicotinamide mononucleotide inhibits post-ischemic NAD+ degradation and dramatically ameliorates brain damage following global cerebral ischemia
Park, J. H., Long, A. N., Owens, K., & Kristián, T. (2016) · Neurobiology of Disease · doi:10.1016/j.nbd.2016.07.018 · Cited by 121 · see citing works
Nicotinamide riboside kinases display redundancy in mediating nicotinamide mononucleotide and nicotinamide riboside metabolism in skeletal muscle cells
Fletcher, R. S., Ratajczak, J., Doig, C. L., Oakey, L. A., Callingham, R., Xavier, G. D. S., Garten, A., Elhassan, Y., Redpath, P., Migaud, M. E., et al. (2017) · Molecular Metabolism · doi:10.1016/j.molmet.2017.05.011 · Cited by 121 · see citing works
PARP-1 Inhibition Prevents Oxidative and Nitrosative Stress–Induced Endothelial Cell Death via Transactivation of the VEGF Receptor 2
Mathews, M. T., & Berk, B. C. (2008) · Arteriosclerosis, Thrombosis, and Vascular Biology · doi:10.1161/atvbaha.107.156406 · Cited by 120 · see citing works
Nicotinamide Offers Multiple Protective Mechanisms in Stroke as a Precursor for NAD+, as a PARP Inhibitor and by Partial Restoration of Mitochondrial Function
Klaidman, L. K., Morales, M., Kem, S., Yang, J., Chang, M., & Adams, J. D., Jr. (2003) · Pharmacology · doi:10.1159/000072668 · Cited by 120 · see citing works
Transport of Nicotinate and Structurally Related Compounds by Human SMCT1 (SLC5A8) and Its Relevance to Drug Transport in the Mammalian Intestinal Tract
Gopal, E., Miyauchi, S., Martin, P. M., Ananth, S., Roon, P., Smith, S. B., & Ganapathy, V. (2007) · Pharmaceutical Research · doi:10.1007/s11095-006-9176-1 · Cited by 118 · see citing works
Leishmania infantum Modulates Host Macrophage Mitochondrial Metabolism by Hijacking the SIRT1-AMPK Axis
Moreira, D., Rodrigues, V., Abengózar, M. Á., Rivas, L., Rial, E., Laforge, M., Li, X., Foretz, M., Viollet, B., Estaquier, J., et al. (2015) · PLoS Pathogens · doi:10.1371/journal.ppat.1004684 · Cited by 116 · see citing works
Nicotinamide Phosphoribosyltransferase/Visfatin Does Not Catalyze Nicotinamide Mononucleotide Formation in Blood Plasma
Hara, N., Yamada, K., Shibata, T., Osago, H., & Tsuchiya, M. (2011) · PLoS ONE · doi:10.1371/journal.pone.0022781 · Cited by 116 · see citing works
Prevention of photoimmunosuppression and photocarcinogenesis by topical nicotinamide
Gensler, H. L. (1997) · Nutrition and Cancer · doi:10.1080/01635589709514618 · Cited by 115 · see citing works
The renoprotective effect of curcumin in cisplatin-induced nephrotoxicity
Ugur, S., Ulu, R., Doğukan, A., Gürel, A., Yiğit, İ. P., Gözel, N., Aygen, B., & İlhan, A. (2015) · Renal Failure · doi:10.3109/0886022x.2014.986005 · Cited by 112 · see citing works
Nicotinamide Riboside Is a Major NAD+ Precursor Vitamin in Cow Milk
Trammell, S. A., Yu, L., Redpath, P., Migaud, M. E., & Brenner, C. (2016) · The Journal of Nutrition · doi:10.3945/jn.116.230078 · Cited by 112 · see citing works
The Adipokine Visfatin is Markedly Elevated in Obese Children
Haider, D. G., Holzer, G., Schaller, G., Weghuber, D., Widhalm, K., Wagner, O. F., Kapiotis, S., & Wolzt, M. (2006) · Journal of Pediatric Gastroenterology and Nutrition · doi:10.1097/01.mpg.0000235749.50820.b3 · Cited by 111 · see citing works
PARP1 Inhibitors: Antitumor Drug Design
Maluchenko, N. V., Kotova, E. Y., Kulaeva, O. I., Kirpichnikov, M. P., & Studitskiy, V. M. (2015) · Acta Naturae · doi:10.32607/20758251-2015-7-3-27-37 · Cited by 111 · see citing works
Human CD38 is an authentic NAD(P)+ glycohydrolase
Berthelier, V., Tixier, J. M., Muller‐Steffner, H., Schuber, F. J., & Déterre, P. (1998) · Biochemical Journal · doi:10.1042/bj3301383 · Cited by 109 · see citing works
Nicotinamide Mononucleotide Pyrophosphorylase Activity in Animal Tissues
Dietrich, L. S., Fuller, L., Yero, I. L., & Martínez, L. A. (1966) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)96977-2 · Cited by 108 · see citing works
Nicotinamide reduces infarction up to two hours after the onset of permanent focal cerebral ischemia in Wistar rats
Ayoub, I. A., Lee, E. J., Ogilvy, C. S., Beal, M. F., & Maynard, K. I. (1999) · Neuroscience Letters · doi:10.1016/s0304-3940(98)00881-7 · Cited by 107 · see citing works
Nicotinamide adenine dinucleotide biosynthesis promotes liver regeneration
Mukherjee, S., Chellappa, K., Moffitt, A. B., Ndungu, J., Dellinger, R. W., Davis, J. G., Agarwal, B., & Baur, J. A. (2016) · Hepatology · doi:10.1002/hep.28912 · Cited by 107 · see citing works
The alcoholic ferment of yeast-juice. Part II.—The coferment of yeast-juice
Harden, A., & Young, W. J. (1906) · Proceedings of the Royal Society of London Series B Containing Papers of a Biological Character · doi:10.1098/rspb.1906.0070 · Cited by 106 · see citing works
Peroxisome Proliferator-activated Receptor (PPAR)-2 Controls Adipocyte Differentiation and Adipose Tissue Function through the Regulation of the Activity of the Retinoid X Receptor/PPARγ Heterodimer
Bai, P., Houten, S. M., Huber, A., Schreiber, V., 渡辺, 光., Kiss, B., de MURCIA, G., Auwerx, J. H., & Murcia, J. M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m701021200 · Cited by 105 · see citing works
Regulation of Poly(ADP-ribose) Polymerase-1-dependent Gene Expression through Promoter-directed Recruitment of a Nuclear NAD+ Synthase
Zhang, T., Berrocal, J. G., Yao, J., DuMond, M. E., Krishnakumar, R., Ruhl, D. D., Ryu, K. W., Gamble, M. J., & Kraus, W. L. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.304469 · Cited by 105 · see citing works
PARP inhibitors in ovarian cancer: evidence, experience and clinical potential
Evans, T., & Matulonis, U. A. (2017) · Therapeutic Advances in Medical Oncology · doi:10.1177/1758834016687254 · Cited by 105 · see citing works
Flavonoids as inhibitors of human CD38
Kellenberger, E., Kuhn, I., Schuber, F. J., & Muller‐Steffner, H. (2011) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2011.05.022 · Cited by 104 · see citing works
Pharmacologic doses of nicotinamide in the treatment of inflammatory skin conditions: a review.
Niren, N. M. (2006) · PubMed · Cited by 101 · see citing works
RNA Regulation by Poly(ADP-Ribose) Polymerases
Bock, F. J., Kwan, T. T., & Chang, P. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.01.037 · Cited by 100 · see citing works

Flagged first, then by citations

Sorted by citations

Cellular senescence and senolytics: the path to the clinic
Chaib, S., Tchkonia, T., & Kirkland, J. L. (2022) · Nature Medicine · doi:10.1038/s41591-022-01923-y · Cited by 1,105 · see citing works
Mitochondrial and metabolic dysfunction in ageing and age-related diseases
Amorim, J. A., Coppotelli, G., Rolo, A. P., Palmeira, C. M., Ross, J. M., & Sinclair, D. A. (2022) · Nature Reviews Endocrinology · doi:10.1038/s41574-021-00626-7 · Cited by 990 · see citing works
Self-citation
NAD+ homeostasis in health and disease
Katsyuba, E., Romani, M., Hofer, D., & Auwerx, J. (2020) · Nature Metabolism · doi:10.1038/s42255-019-0161-5 · Cited by 627 · see citing works
Caloric Restriction Mimetics against Age-Associated Disease: Targets, Mechanisms, and Therapeutic Potential
Madeo, F., Carmona-Gutierrez, D., Hofer, S. J., & Kroemer, G. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2019.01.018 · Cited by 630 · see citing works
Immunosenescence: a key player in cancer development
Lian, J., Yue, Y., Yu, W., & Zhang, Y. (2020) · Journal of Hematology & Oncology · doi:10.1186/s13045-020-00986-z · Cited by 510 · see citing works
The quest to slow ageing through drug discovery
Partridge, L., Fuentealba, M., & Kennedy, B. K. (2020) · Nature Reviews Drug Discovery · doi:10.1038/s41573-020-0067-7 · Cited by 468 · see citing works
Extracellular vesicle-contained eNAMPT delays aging and extends lifespan in mice
Yoshida, M., Satoh, A., Lin, J. B., Mills, K. F., Sasaki, Y., Rensing, N., Wong, M., Apte, R. S., & Imai, S.-I. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2019.05.015 · Cited by 407 · see citing works
Mitochondrial oxidative capacity and NAD+ biosynthesis are reduced in human sarcopenia across ethnicities
Migliavacca, E., Tay, S. K. H., Patel, H. P., Sonntag, T., Civiletto, G., McFarlane, C., Forrester, T., Barton, S. J., Leow, M. K., Antoun, E., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-13694-1 · Cited by 365 · see citing works
The NAD+ precursor nicotinamide riboside rescues mitochondrial defects and neuronal loss in iPSC and fly models of Parkinson's disease
Schöndorf, D. C., Ivanyuk, D., Baden, P., Sanchez-Martinez, A., De Cicco, S., Yu, C., Giunta, I., Schwarz, L. K., Di Napoli, G., Panagiotakopoulou, V., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.05.009 · Cited by 337 · see citing works
Mitochondrial Dysfunction, Oxidative Stress, Neuroinflammation, and Metabolic Alterations in the Progression of Alzheimer's Disease: A Meta-Analysis of In Vivo Magnetic Resonance Spectroscopy Studies
Song, T., Song, X., Zhu, C., Patrick, R., Skurla, M., Santangelo, I., Green, M., Harper, D., Ren, B., Forester, B. P., et al. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101503 · Cited by 346 · see citing works
Slc12a8 is a nicotinamide mononucleotide transporter
Grozio, A., Mills, K. F., Yoshino, J., Bruzzone, S., Sociali, G., Tokizane, K., Lei, H. C., Cunningham, R., Sasaki, Y., Migaud, M. E., et al. (2019) · Nature Metabolism · doi:10.1038/s42255-018-0009-4 · Cited by 287 · see citing works
NAD metabolism: Implications in aging and longevity
Yaku, K., Okabe, K., & Nakagawa, T. (2018) · Ageing Research Reviews · doi:10.1016/j.arr.2018.05.006 · Cited by 269 · see citing works
Bacteria Boost Mammalian Host NAD Metabolism by Engaging the Deamidated Biosynthesis Pathway
Shats, I., Williams, J. G., Liu, J., Makarov, M. V., Wu, X., Lih, F. B., Deterding, L. J., Lim, C., Xu, X., Randall, T. A., et al. (2020) · Cell Metabolism · doi:10.1016/j.cmet.2020.02.001 · Cited by 242 · see citing works
Implications of altered NAD metabolism in metabolic disorders
Okabe, K., Yaku, K., Tobe, K., & Nakagawa, T. (2019) · Journal of Biomedical Science · doi:10.1186/s12929-019-0527-8 · Cited by 223 · see citing works
MCART1/SLC25A51 is required for mitochondrial NAD transport
Kory, N., uit de Bos, J., van der Rijt, S., Jankovic, N., Güra, M., Arp, N., Pena, I. A., Prakash, G., Chan, S. H., Kunchok, T., et al. (2020) · Science Advances · doi:10.1126/sciadv.abe5310 · Cited by 205 · see citing works
Boosting NAD+ with a small molecule that activates NAMPT
Gardell, S. J., Hopf, M., Khan, A., Dispagna, M., Hampton Sessions, E., Falter, R., Kapoor, N., Brooks, J., Culver, J., Petucci, C., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-11078-z · Cited by 169 · see citing works
Systematic review and analysis of human proteomics aging studies unveils a novel proteomic aging clock and identifies key processes that change with age
Johnson, A. A., Shokhirev, M. N., Wyss-Coray, T., & Lehallier, B. (2020) · Ageing Research Reviews · doi:10.1016/j.arr.2020.101070 · Cited by 166 · see citing works
Nicotinamide riboside does not alter mitochondrial respiration, content or morphology in skeletal muscle from obese and insulin‐resistant men
Dollerup, O. L., Chubanava, S., Agerholm, M., Søndergård, S. D., Altıntaş, A., Møller, A. B., Høyer, K. F., Ringgaard, S., Stødkilde‐Jørgensen, H., Lavery, G. G., et al. (2020) · The Journal of Physiology · doi:10.1113/jp278752 · Cited by 145 · see citing works
Metformin Is a Direct SIRT1-Activating Compound: Computational Modeling and Experimental Validation
Cuyàs, E., Verdura, S., Llorach-Parés, L., Fernández-Arroyo, S., Joven, J., Martin-Castillo, B., Bosch-Barrera, J., Brunet, J., Nonell-Canals, A., Sanchez-Martinez, M., et al. (2018) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00657 · Cited by 122 · see citing works
The road ahead for health and lifespan interventions
Gonzalez-Freire, M., Diaz-Ruiz, A., Hauser, D., Martinez-Romero, J., Ferrucci, L., Bernier, M., & de Cabo, R. (2020) · Ageing Research Reviews · doi:10.1016/j.arr.2020.101037 · Cited by 118 · see citing works
Caloric Restriction Mimetics in Nutrition and Clinical Trials
Hofer, S. J., Davinelli, S., Bergmann, M., Scapagnini, G., & Madeo, F. (2021) · Frontiers in Nutrition · doi:10.3389/fnut.2021.717343 · Cited by 109 · see citing works
Healthy aging and muscle function are positively associated with NAD+ abundance in humans
Janssens, G. E., Grevendonk, L., Perez, R. Z., Schomakers, B. V., de Vogel-van den Bosch, J., Geurts, J. M. W., van Weeghel, M., Schrauwen, P., Houtkooper, R. H., & Hoeks, J. (2022) · Nature Aging · doi:10.1038/s43587-022-00174-3 · Cited by 103 · see citing works
Effects of Nicotinamide Riboside on Endocrine Pancreatic Function and Incretin Hormones in Nondiabetic Men With Obesity
Dollerup, O. L., Trammell, S. A. J., Hartmann, B., Holst, J. J., Christensen, B., Møller, N., Gillum, M. P., Treebak, J. T., & Jessen, N. (2019) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2019-01081 · Cited by 77 · see citing works
BST1 regulates nicotinamide riboside metabolism via its glycohydrolase and base-exchange activities
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Background
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Authors: Rajman, L., Chwalek, K., & Sinclair, D. A.
Affiliations: Harvard University (US)
Corresponding author: Sinclair, David A.
ORCID: Rajman, Luis
Chwalek, Karolina
Sinclair, David A.
Venue: Cell Metabolism
Publisher: Elsevier BV
Published: 2018-03
Volume: 27
Issue: 3
Pages: 529-547
ISSN: 1550-4131 (ISSN-L)
DOI: 10.1016/j.cmet.2018.02.011
PMC: PMC6342515
OpenAlex: W2791758888
Cited by: 865
References: 270
Citations by year: 2026: 81 · 2025: 105 · 2024: 132 · 2023: 113 · 2022: 122 · 2021: 123 · 2020: 106 · 2019: 56 · 2018: 25
FWCI: 8.63
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 370 d)
Locations: Cell Metabolism (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
Funders: National Institute on Aging (DP1AG058605, R37AG028730, R01AG019719)
National Institute of Diabetes and Digestive and Kidney Diseases (R01DK100263)
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+, NAD+ precursors, aging, lifespan extension, healthy aging, in vivo evidence, metabolic resilience
MeSH terms: Animals, Energy Metabolism, Humans, Longevity, NAD, Signal Transduction

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Therapeutic Potential of NAD-Boosting Molecules: The In Vivo Evidence

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