Resistance training increases muscle NAD(+) and NADH concentrations as well as NAMPT protein levels and global sirtuin activity in middle-aged, overweight, untrained individuals

Transcriptional 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 · see citing works

SIRT3 regulates mitochondrial fatty-acid oxidation by reversible enzyme deacetylation

Hirschey, M. D., Shimazu, T., Goetzman, E., Jing, E., Schwer, B., Lombard, D. B., Grueter, C. A., Harris, C., Biddinger, S., Ilkayeva, O. R., et al. (2010) · Nature · doi:10.1038/nature08778 · Cited by 1,687 · 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

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

Regulation of pgc-1α, a nodal regulator of mitochondrial biogenesis

Fernandez-Marcos, P. J., & Auwerx, J. (2011) · The American Journal of Clinical Nutrition · doi:10.3945/ajcn.110.001917 · Cited by 1,237 · 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

Biomarkers of mitochondrial content in skeletal muscle of healthy young human subjects

Larsen, S., Nielsen, J., Hansen, C. N., Nielsen, L. B., Wibrand, F., Stride, N., Schroder, H. D., Boushel, R., Helge, J. W., Dela, F., et al. (2012) · The Journal of Physiology · doi:10.1113/jphysiol.2012.230185 · Cited by 1,180 · 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

The NAD Biosynthesis Pathway Mediated by Nicotinamide Phosphoribosyltransferase Regulates Sir2 Activity in Mammalian Cells

Revollo, J. R., Grimm, A. A., & Imai, S.-I. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408388200 · Cited by 1,010 · see citing works

NAD+ metabolism in health and disease

Belenky, P. A., Bogan, K. L., & Brenner, C. (2006) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2006.11.006 · Cited by 983 · 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

Nicotinamide riboside is uniquely and orally bioavailable in mice and humans

Trammell, S. A. J., Schmidt, M. S., Weidemann, B. J., Redpath, P., Jaksch, F., Dellinger, R. W., Li, Z., Abel, E. D., Migaud, M. E., & Brenner, C. (2016) · Nature Communications · doi:10.1038/ncomms12948 · Cited by 697 · see citing works

Regulation of activity of the transcription factor GATA-1 by acetylation

Boyes, J., Byfield, P., Nakatani, Y., & Ogryzko, V. (1998) · Nature · doi:10.1038/25166 · Cited by 694 · 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

Enhanced Protein Translation Underlies Improved Metabolic and Physical Adaptations to Different Exercise Training Modes in Young and Old Humans

Robinson, M. M., Dasari, S., Konopka, A. R., Johnson, M. L., Manjunatha, S., Esponda, R. R., Carter, R. E., Lanza, I. R., & Nair, K. S. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2017.02.009 · Cited by 539 · see citing works

Nicotinamide Riboside Augments the Aged Human Skeletal Muscle NAD+ Metabolome and Induces Transcriptomic and Anti-inflammatory Signatures

Elhassan, Y. S., Kluckova, K., Fletcher, R. S., Schmidt, M. S., Garten, A., Doig, C. L., Cartwright, D. M., Oakey, L., Burley, C. V., Jenkinson, N., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.07.043 · Cited by 448 · see citing works

Cell cycle-dependent deacetylation of telomeric histone H3 lysine K56 by human SIRT6

Michishita, E., McCord, R. A., Boxer, L. D., Barber, M. F., Hong, T., Gozani, O., & Chua, K. F. (2009) · Cell Cycle · doi:10.4161/cc.8.16.9367 · Cited by 384 · 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

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

Resistance exercise training alters mitochondrial function in human skeletal muscle

PORTER, C., REIDY, P. T., BHATTARAI, N., SIDOSSIS, L. S., & RASMUSSEN, B. B. (2015) · Medicine & Science in Sports & Exercise · doi:10.1249/mss.0000000000000605 · Cited by 288 · see citing works

Reconstructing eukaryotic NAD metabolism.

Rongvaux, A., Andris, F., Gool, F. V., & Leo, O. (2003) · Bioessays · doi:10.1002/bies.10297 · Cited by 284 · 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

Sirt3 regulates metabolic flexibility of skeletal muscle through reversible enzymatic deacetylation

Jing, E., O’Neill, B. T., Rardin, M. J., Kleinridders, A., Ilkeyeva, O. R., Ussar, S., Bain, J. R., Lee, K. Y., Verdin, E. M., Newgard, C. B., et al. (2013) · Diabetes · doi:10.2337/db12-1650 · Cited by 283 · see citing works

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

Structural basis for sirtuin function: What we know and what we don't

Sanders, B. D., Jackson, B. A., & Marmorstein, R. (2009) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2009.09.009 · Cited by 245 · see citing works

SIRT1 Controls the Transcription of the Peroxisome Proliferator-activated Receptor-γ Co-activator-1α (PGC-1α) Gene in Skeletal Muscle through the PGC-1α Autoregulatory Loop and Interaction with MyoD

Amat, R., Planavila, A., Chen, S. L., Iglesias, R., Giralt, M., & Villarroya, F. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.022749 · Cited by 218 · see citing works

Resistance exercise training decreases oxidative damage to DNA and increases cytochrome oxidase activity in older adults

Parise, G., BROSE, A., & Tarnopolsky, M. G. (2004) · Experimental Gerontology · doi:10.1016/j.exger.2004.09.002 · Cited by 196 · see citing works

Endurance exercise increases the SIRT1 and peroxisome proliferator-activated receptor γ coactivator-1α protein expressions in rat skeletal muscle

Suwa, M., Nakano, H., Radak, Z. O., & Kumagai, S. (2008) · Metabolism · doi:10.1016/j.metabol.2008.02.017 · Cited by 195 · see citing works

A critical evaluation of the biological construct skeletal muscle hypertrophy: size matters but so does the measurement

Haun, C. T., Vann, C. G., Roberts, B. M., Vigotsky, A. D., Schoenfeld, B. J., & Roberts, M. D. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00247 · Cited by 192 · see citing works

Mitochondrial volume density in human skeletal muscle following heavy resistance training.

Jd, M., SALE, D. G., Мороз, Gc, E., Sutton, M. A., & HOWALD, H. (1979) · PubMed · Cited by 191 · see citing works

Resistance exercise enhances the molecular signaling of mitochondrial biogenesis induced by endurance exercise in human skeletal muscle

Wang, L., Mascher, H., Psilander, N., Blomstrand, E., & Sahlin, K. (2011) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00086.2011 · Cited by 181 · see citing works

Antioxidant enzyme activity is up-regulated after unilateral resistance exercise training in older adults

Parise, G., Phillips, S. M., Kaczor, J. J., & Tarnopolsky, M. A. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.03.024 · Cited by 174 · see citing works

DNA damage-induced PARP1 activation confers cardiomyocyte dysfunction through NAD+ depletion in experimental atrial fibrillation

Zhang, D., Hu, X., Li, J., Liu, J., Bulte, L. B.-T., Wiersma, M., Malik, N.-U.-A., van Marion, D. M. S., Tolouee, M., Hoogstra‐Berends, F., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-09014-2 · Cited by 163 · 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

Age-Associated Impairments in Mitochondrial ADP Sensitivity Contribute to Redox Stress in Senescent Human Skeletal Muscle

Holloway, G. P., Holwerda, A. M., Miotto, P. M., Dirks, M. L., Verdijk, L. B., & van Loon, L. J. C. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.02.069 · Cited by 134 · see citing works

High-intensity interval training increases SIRT1 activity in human skeletal muscle

Gurd, B. J., Perry, C. G. R., Heigenhauser, G. J. F., Spriet, L. L., & Bonen, A. (2010) · Applied Physiology, Nutrition, and Metabolism · doi:10.1139/h10-030 · Cited by 128 · see citing works

Increased muscle oxidative potential following resistance training induced fibre hypertrophy in young men

Tang, J. E., Hartman, J. W., & Phillips, S. M. (2006) · Applied Physiology, Nutrition, and Metabolism · doi:10.1139/h06-026 · Cited by 116 · see citing works

Biomarkers associated with low, moderate, and high vastus lateralis muscle hypertrophy following 12 weeks of resistance training

Mobley, C. B., Haun, C. T., Roberson, P. A., Mumford, P. W., Kephart, W. C., Romero, M. A., Osburn, S. C., Vann, C. G., Young, K. C., Beck, D. T., et al. (2018) · PLOS ONE · doi:10.1371/journal.pone.0195203 · Cited by 112 · see citing works

AMP‐activated protein kinase regulates nicotinamide phosphoribosyl transferase expression in skeletal muscle

Brandauer, J., Vienberg, S. G., Agerholm, M., Ringholm, S., Risis, S., Larsen, P. S., Kristensen, J. M., Frøsig, C., Leick, L., Fentz, J., et al. (2013) · The Journal of Physiology · doi:10.1113/jphysiol.2013.259515 · Cited by 105 · see citing works

Enzymatic adaptations consequent to long-term strength training

Tesch, P., Komi, P., & Häkkinen, K. (1987) · International Journal of Sports Medicine · doi:10.1055/s-2008-1025706 · Cited by 101 · see citing works

Aerobic and resistance exercise training reverses age‐dependent decline in NAD⁺salvage capacity in human skeletal muscle

de Guia, R. M., Agerholm, M., Nielsen, T. S., Consitt, L. A., Søgaard, D., Helge, J. W., Larsen, S., Brandauer, J., Houmard, J. A., & Treebak, J. T. (2019) · Physiological Reports · doi:10.14814/phy2.14139 · Cited by 99 · see citing works

Muscle fiber hypertrophy in response to 6 weeks of high-volume resistance training in trained young men is largely attributed to sarcoplasmic hypertrophy

Haun, C. T., Vann, C. G., Osburn, S. C., Mumford, P. W., Roberson, P. A., Romero, M. A., Fox, C. D., Johnson, C. A., Parry, H. A., Kavazis, A. N., et al. (2019) · PLoS ONE · doi:10.1371/journal.pone.0215267 · Cited by 95 · see citing works

Human Skeletal Muscle Mitochondrial Adaptations Following Resistance Exercise Training

Parry, H. A., Roberts, M. D., & Kavazis, A. N. (2020) · International Journal of Sports Medicine · doi:10.1055/a-1121-7851 · Cited by 92 · see citing works

A need for NAD+ in muscle development, homeostasis, and aging

Goody, M. F., & Henry, C. A. (2018) · Skeletal Muscle · doi:10.1186/s13395-018-0154-1 · Cited by 75 · see citing works

The effect of strength training on estimates of mitochondrial density and distribution throughout muscle fibres

Chilibeck, P. D., Syrotuik, D. G., & Bell, G. J. (1999) · European Journal of Applied Physiology and Occupational Physiology · doi:10.1007/s004210050641 · Cited by 74 · see citing works

Ten weeks of branched-chain amino acid supplementation improves select performance and immunological variables in trained cyclists

Kephart, W. C., Wachs, T. D., Mac Thompson, R., Brooks Mobley, C., Fox, C. D., McDonald, J. R., Ferguson, B. S., Young, K. C., Nie, B., Martin, J. S., et al. (2016) · Amino Acids · doi:10.1007/s00726-015-2125-8 · Cited by 62 · see citing works

Pre-training Skeletal Muscle Fiber Size and Predominant Fiber Type Best Predict Hypertrophic Responses to 6 Weeks of Resistance Training in Previously Trained Young Men

Haun, C. T., Vann, C. G., Mobley, C. B., Osburn, S. C., Mumford, P. W., Roberson, P. A., Romero, M. A., Fox, C. D., Parry, H. A., Kavazis, A. N., et al. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00297 · Cited by 60 · see citing works

Pro-renin receptor suppresses mitochondrial biogenesis and function via AMPK/SIRT-1/ PGC-1α pathway in diabetic kidney

Akhtar, S., & Siragy, H. M. (2019) · PLoS ONE · doi:10.1371/journal.pone.0225728 · Cited by 57 · see citing works

The NAMPT Promoter Is Regulated by Mechanical Stress, Signal Transducer and Activator of Transcription 5, and Acute Respiratory Distress Syndrome–Associated Genetic Variants

Sun, X., Elangovan, V. R., Mapes, B. L., et al. (2014) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2014-0117oc · Cited by 56 · see citing works

A randomized 3-way crossover study indicates that high-protein feeding induces de novo lipogenesis in healthy humans

Charidemou, E., Ashmore, T., Li, X., McNally, B. D., West, J. A., Liggi, S., Harvey, M., Orford, E., & Griffin, J. L. (2019) · JCI Insight · doi:10.1172/jci.insight.124819 · Cited by 52 · see citing works

Skeletal muscle mitochondrial volume and myozenin-1 protein differences exist between high versus low anabolic responders to resistance training

Roberts, M. D., Romero, M. A., Mobley, C. B., Mumford, P. W., Roberson, P. A., Haun, C. T., Vann, C. G., Osburn, S. C., Holmes, H. H., Greer, R. A., et al. (2018) · PeerJ · doi:10.7717/peerj.5338 · Cited by 50 · see citing works

Molecular, neuromuscular, and recovery responses to light versus heavy resistance exercise in young men

Haun, C. T., Mumford, P. W., Roberson, P. A., Romero, M. A., Mobley, C. B., Kephart, W. C., Anderson, R. G., Colquhoun, R. J., Muddle, T. W. D., Luera, M. J., et al. (2017) · Physiological Reports · doi:10.14814/phy2.13457 · Cited by 48 · see citing works

A high-throughput pipeline for validation of antibodies

Sikorski, K., Mehta, A., Inngjerdingen, M., Thakor, F. K., Kling, S., Kalina, T., Nyman, T. A., Stensland, M., Zhou, W., de Souza, G. A., et al. (2018) · Nature Methods · doi:10.1038/s41592-018-0179-8 · Cited by 40 · see citing works

Ketones improves Apolipoprotein E4-related memory deficiency via sirtuin 3

Yin, J., Nielsen, M., Li, S., & Shi, J. (2019) · Aging · doi:10.18632/aging.102070 · Cited by 35 · see citing works

A single bout of whole‐leg, peristaltic pulse external pneumatic compression upregulates PGC‐1α mRNA and endothelial nitric oxide sythase protein in human skeletal muscle tissue

Kephart, W. C., Mobley, C. B., Fox, C. D., Pascoe, D. D., Sefton, J. M., Wilson, T. J., Goodlett, M. D., Kavazis, A. N., Roberts, M. D., & Martin, J. S. (2015) · Experimental Physiology · doi:10.1113/ep085160 · Cited by 32 · see citing works

Influence of resistance exercise intensity and metabolic stress on anabolic signaling and expression of myogenic genes in skeletal muscle

Popov, D. V., Lysenko, E. A., Bachinin, A. V., Miller, T. F., Kurochkina, N. S., Kravchenko, I. V., Furalyov, V. A., & Vinogradova, O. L. (2015) · Muscle & Nerve · doi:10.1002/mus.24314 · Cited by 32 · see citing works

Antioxidant and Cardioprotective Effects of EPA on Early Low-Severity Sepsis through UCP3 and SIRT3 Upholding of the Mitochondrial Redox Potential

Léger, T., Azarnoush, K., Traoré, A. S., Cassagnes, L., Rigaudière, J., Jouve, C., Pagés, G., Bouvier, D., Sapin, V., Pereira, B., et al. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/9710352 · Cited by 30 · see citing works

Pharmacological NAD-Boosting Strategies Improve Mitochondrial Homeostasis in Human Complex I–Mutant Fibroblasts

Felici, R., Lapucci, A., Cavone, L., Pratesi, S., Palmini, R. B., & Chiarugi, A. (2015) · Molecular Pharmacology · doi:10.1124/mol.114.097204 · Cited by 28 · see citing works

Ginsenoside Rg1 attenuates isoflurane/surgery-induced cognitive disorders and sirtuin 3 dysfunction

Miao, H., Wang, M., Wang, H., et al. (2019) · Bioscience Reports · doi:10.1042/bsr20190069 · Cited by 21 · see citing works

Salidroside protects PC12 cells from Aβ1–40-induced cytotoxicity by regulating the nicotinamide phosphoribosyltransferase signaling pathway

Huang, X., Xing, S., Chen, C., Yu, Z., & Chen, J. (2017) · Molecular Medicine Reports · doi:10.3892/mmr.2017.6931 · Cited by 14 · see citing works

A novel form of Deleted in breast cancer 1 (DBC1) lacking the N-terminal domain does not bind SIRT1 and is dynamically regulated in vivo

dos Santos, L. F. V., Colman, L., Contreras, P., Chini, C. C. S., Carlomagno, A., Leyva, A., Bresque, M., Marmisolle, I., Quijano, C., Durán, R., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-50789-7 · Cited by 9 · see citing works

Acute and chronic effects of resistance training on skeletal muscle markers of mitochondrial remodeling in older adults

Mesquita, P. H. C., Lamb, D. A., Parry, H. A., Moore, J. H., Smith, M. A., Vann, C. G., Osburn, S. C., Fox, C. D., Ruple, B. A., Huggins, K. W., et al. (2020) · Physiological Reports · doi:10.14814/phy2.14526 · Cited by 66 · see citing works

Skeletal Muscle Ribosome and Mitochondrial Biogenesis in Response to Different Exercise Training Modalities

Mesquita, P. H. C., Vann, C. G., Phillips, S. M., McKendry, J., Young, K. C., Kavazis, A. N., & Roberts, M. D. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.725866 · Cited by 62 · see citing works

Pre-training Skeletal Muscle Fiber Size and Predominant Fiber Type Best Predict Hypertrophic Responses to 6 Weeks of Resistance Training in Previously Trained Young Men

Haun, C. T., Vann, C. G., Mobley, C. B., Osburn, S. C., Mumford, P. W., Roberson, P. A., Romero, M. A., Fox, C. D., Parry, H. A., Kavazis, A. N., et al. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00297 · Cited by 60 · see citing works

Exercise training upregulates intracellular nicotinamide phosphoribosyltransferase expression in humans: a systematic review with meta-analysis

Sun, X., Su, L., Bu, T., & Zhang, Y. (2023) · Frontiers in Public Health · doi:10.3389/fpubh.2023.1287421 · Cited by 10 · see citing works

Mutations that Allow SIR2 Orthologs to Function in a NAD+-Depleted Environment

Ondracek, C. R., Frappier, V., Ringel, A. E., Wolberger, C., & Guarente, L. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.02.031 · Cited by 18 · see citing works

Free [NADH]/[NAD+] regulates sirtuin expression

Gambini, J., Gómez‐Cabrera, M. C., Borrás, C., Vallés, S. L., López-Grueso, R., Martinez-Bello, V. E., Herranz, D., Pallardó, F. V., Tresguerres, J. A. F., Serrano, M., et al. (2011) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2011.04.020 · Cited by 47 · see citing works

Metabolic control by sirtuins and other enzymes that sense NAD+, NADH, or their ratio

Anderson, K. A., Madsen, A. S., Olsen, C. A., & Hirschey, M. D. (2017) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2017.09.005 · Cited by 210 · see citing works

NAD+ as a Pharmacological Tool to Boost Sirtuin Activity

Houtkooper, R. H. (2016) · Springer eBooks · doi:10.1007/978-94-024-0962-8_2

NAD metabolism and sirtuins: Metabolic regulation of protein deacetylation in stress and toxicity

Yang, T., & Sauve, A. A. (2006) · The AAPS Journal · doi:10.1208/aapsj080472 · Cited by 170 · see citing works