Nicotinamide Riboside and Nicotinic Acid Riboside Salvage in Fungi and Mammals
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NAD+ is a co-enzyme for hydride transfer enzymes and an essential substrate of ADP-ribose transfer enzymes and sirtuins, the type III protein lysine deacetylases related to yeast Sir2. Supplementation of yeast cells with nicotinamide riboside extends replicative lifespan and increases Sir2-dependent gene silencing by virtue of increasing net NAD+ synthesis. Nicotinamide riboside elevates NAD+ levels via the nicotinamide riboside kinase pathway and by a pathway initiated by splitting the nucleoside into a nicotinamide base followed by nicotinamide salvage. Genetic evidence has established that uridine hydrolase, purine nucleoside phosphorylase, and methylthioadenosine phosphorylase are required for Nrk-independent utilization of nicotinamide riboside in yeast. Here we show that mammalian purine nucleoside phosphorylase but not methylthioadenosine phosphorylase is responsible for mammalian nicotinamide riboside kinase-independent nicotinamide riboside utilization. We demonstrate that so-called uridine hydrolase is 100-fold more active as a nicotinamide riboside hydrolase than as a uridine hydrolase and that uridine hydrolase and mammalian purine nucleoside phosphorylase cleave nicotinic acid riboside, whereas the yeast phosphorylase has little activity on nicotinic acid riboside. Finally, we show that yeast nicotinic acid riboside utilization largely depends on uridine hydrolase and nicotinamide riboside kinase and that nicotinic acid riboside bioavailability is increased by ester modification.
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Most bacteria have a NAM deamidase, an enzyme that converts NAM into NA.
“Most bacteria have a NAM deamidase, an enzyme that converts NAM into NA.”
From Nicotinamide riboside and nicotinamide mononucleotide facilitate NAD <sup>+</sup> synthesis via enterohepatic circulation (2025) · cites this paper as [12]
Mammals do not have a homologous enzyme to NAM deamidase.
“However, mammals do not have a homologous enzyme (12, 25–28).”
From Nicotinamide riboside and nicotinamide mononucleotide facilitate NAD <sup>+</sup> synthesis via enterohepatic circulation (2025) · cites this paper as [12]
NR is converted to NMN by NR kinase (NRK), thereby bypassing the NAMPT-mediated step.
“Meanwhile, NR is converted to NMN by NR kinase (NRK), thereby bypassing the NAMPT-mediated step (11, 12).”
From Nicotinamide riboside and nicotinamide mononucleotide facilitate NAD <sup>+</sup> synthesis via enterohepatic circulation (2025) · cites this paper as [12]
Cites
Global analysis of protein expression in yeast
Ghaemmaghami, S., Huh, W.-K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., & Weissman, J. S. (2003) · Nature · doi:10.1038/nature02046 · Cited by 3,750 · see citing works
Poly(ADP-ribose): novel functions for an old molecule
Schreiber, V., Dantzer, F., Amé, J., & de MURCIA, G. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1963 · Cited by 1,917 · see citing works
Sirtuins in mammals: insights into their biological function
Michán, S., & Sinclair, D. A. (2007) · Biochemical Journal · doi:10.1042/bj20070140 · Cited by 1,719 · 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
Self-citationCalorie restriction–the SIR2 connection
Guarente, L., & Picard, F. (2005) · Cell · doi:10.1016/j.cell.2005.01.029 · Cited by 793 · see citing works
Bieganowski, P., & Brenner, C. (2004) · Cell · doi:10.1016/s0092-8674(04)00416-7 · Cited by 750 · see citing works
Self-citationSir2 links chromatin silencing, metabolism, and agingPreprint
Guarente, L. (2000) · Genes & Development · doi:10.1101/gad.14.9.1021 · Cited by 718 · see citing works
Smith, J. S., Brachmann, C. B., Celic, I., Kenna, M. A., Muhammad, S., Starai, V. J., Avalos, J. L., Escalante-Semerena, J. C., Grubmeyer, C., Wolberger, C., et al. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.12.6658 · Cited by 718 · see citing works
Bogan, K. L., & Brenner, C. (2008) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.28.061807.155443 · Cited by 707 · see citing works
Self-citationSirtuins in aging and age-related disease
Longo, V. D., & Kennedy, B. K. (2006) · Cell · doi:10.1016/j.cell.2006.07.002 · Cited by 628 · see citing works
Tanner, K. G., Landry, J. W., Sternglanz, R., & Denu, J. M. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.250422697 · Cited by 557 · see citing works
Belenky, P., Racette, F. G., Bogan, K. L., McClure, J. M., Smith, J. S., & Brenner, C. (2007) · Cell · doi:10.1016/j.cell.2007.03.024 · Cited by 411 · see citing works
Self-citationSirtuins: The ‘ <i>magnificent seven</i> ’, function, metabolism and longevity
Dali‐Youcef, N., Lagouge, M., Froelich, S., Koehl, C., Schoonjans, K., & Auwerx, J. (2007) · Annals of Medicine · doi:10.1080/07853890701408194 · Cited by 402 · see citing works
An Enzymatic Activity in the Yeast Sir2 Protein that Is Essential for Gene Silencing
Tanny, J. C., Dowd, G. J., Huang, J., Hilz, H., & Moazed, D. (1999) · Cell · doi:10.1016/s0092-8674(00)81671-2 · Cited by 391 · see citing works
Sirtuins in Aging and DiseasePreprint
Guarente, L. (2007) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2007.72.024 · Cited by 371 · see citing works
Chemistry of Gene Silencing: The Mechanism of NAD+-Dependent Deacetylation Reactions
Sauve, A. A., Celic, I., Avalos, J. L., Deng, H., Boeke, J. D., & Schramm, V. L. (2001) · Biochemistry · doi:10.1021/bi011858j · Cited by 301 · see citing works
Bürkle, A. (2005) · FEBS Journal · doi:10.1111/j.1742-4658.2005.04864.x · Cited by 294 · see citing works
Eng, C., & Mulligan, L. M. (1997) · Human Mutation · doi:10.1002/(sici)1098-1004(1997)9:2 · Cited by 212 · see citing works
Nicotinamide Riboside Kinase Structures Reveal New Pathways to NAD+
Tempel, W., Rabeh, W. M., Bogan, K. L., Belenky, P. A., Wójcik, M., Seidle, H. F., Nedyalkova, L., Yang, T., Sauve, A. A., Park, H.-W., et al. (2007) · PLoS Biology · doi:10.1371/journal.pbio.0050263 · Cited by 163 · see citing works
Self-citationTHE PHOSPHOROLYSIS OF NICOTINAMIDE RIBOSIDE
Rowen, J. W., & Kornberg, A. (1951) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)50905-4 · Cited by 146 · see citing works
Lewandowicz, A., Tyler, P. C., Evans, G. B., Furneaux, R. H., & Schramm, V. L. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.c300259200 · Cited by 126 · see citing works
NAD+ and NADH in brain functions, brain diseases and brain aging
Ying, W. (2006) · Frontiers in bioscience · doi:10.2741/2194 · Cited by 122 · see citing works
Yang, T., Chan, N. Y., & Sauve, A. A. (2007) · Journal of Medicinal Chemistry · doi:10.1021/jm701001c · Cited by 113 · see citing works
Enzymatic Functions and Structures of CD38 and Homologs
Lee, H. C. (2000) · KARGER eBooks · doi:10.1159/000058774 · Cited by 112 · see citing works
Calf Spleen Purine Nucleoside Phosphorylase Complexed with Substrates and Substrate Analogues,
Mao, C., Cook, W. J., Zhou, M., Federov, A., Almo, S. C., & Ealick, S. E. (1998) · Biochemistry · doi:10.1021/bi9723919 · Cited by 104 · see citing works
Enzymology of mammalian NAD metabolism in health and disease
Magni, G. (2008) · Frontiers in bioscience · doi:10.2741/3143 · Cited by 93 · see citing works
Saccharomyces cerevisiae YOR071C Encodes the High Affinity Nicotinamide Riboside Transporter Nrt1
Belenky, P. A., Moga, T. G., & Brenner, C. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.c800021200 · Cited by 78 · see citing works
Self-citationPurine Nucleoside Phosphorylase. 3. Reversal of Purine Base Specificity by Site-Directed Mutagenesis
Stoeckler, J. D., Poirot, A. F., Smith, R. M., Parks, R. E., Ealick, S. E., Takabayashi, K., & Erion, M. D. (1997) · Biochemistry · doi:10.1021/bi961971n · Cited by 78 · see citing works
Bieganowski, P., Pace, H. C., & Brenner, C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302257200 · Cited by 71 · see citing works
Self-citationBieganowski, P., Seidle, H. F., Wójcik, M., & Brenner, C. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m513919200 · Cited by 61 · see citing works
Self-citationThe URH1 uridine ribohydrolase of Saccharomyces cerevisiae
Kurtz, J., Exinger, F., Erbs, P., & Jund, R. (2002) · Current Genetics · doi:10.1007/s00294-002-0296-9 · Cited by 60 · see citing works
Sirtuins: a conserved key unlocking AceCS activity
North, B. J., & Sinclair, D. A. (2006) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2006.11.002 · Cited by 59 · see citing works
Assimilation of NAD + precursors in Candida glabrata
Ma, B., Pan, S., Zupancic, M. L., & Cormack, B. P. (2007) · Molecular Microbiology · doi:10.1111/j.1365-2958.2007.05886.x · Cited by 54 · see citing works
Glutamine-dependent NAD+ Synthetase
Wójcik, M., Seidle, H. F., Bieganowski, P., & Brenner, C. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m607111200 · Cited by 52 · see citing works
Self-citationMagni, G., Fioretti, E., Ipata, P. L., & Natalini, P. (1975) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)41972-8 · Cited by 41 · see citing works
Wielgus‐Kutrowska, B., Kulikowska, E., Wierzchowski, J., Bzowska, A., & Shugar, D. (1997) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1997.0408a.x · Cited by 40 · see citing works
Mitterbauer, R., Karl, T., & Adam, G. (2002) · Applied and Environmental Microbiology · doi:10.1128/aem.68.3.1336-1343.2002 · Cited by 37 · see citing works
Structural Basis for Substrate Specificity in Group I Nucleoside Hydrolases,
Iovane, E., Giabbai, B., Muzzolini, L., Matafora, V., Fornili, A., Minici, C., Giannese, F., & Degano, M. (2008) · Biochemistry · doi:10.1021/bi702448s · Cited by 36 · see citing works
YLR209c Encodes Saccharomyces cerevisiae Purine Nucleoside Phosphorylase
Lecoq, K., Belloc, I., Desgranges, C., Konrad, M., & Daignan‐Fornier, B. (2001) · Journal of Bacteriology · doi:10.1128/jb.183.16.4910-4913.2001 · Cited by 34 · see citing works
Transition state analogues in quorum sensing and SAM recycling
Schramm, V. L., Gutierrez, J. A., Cordovano, G., Basu, I., Guha, C., Belbin, T. J., Evans, G. B., Tyler, P. C., & Furneaux, R. H. (2008) · Nucleic Acids Symposium Series · doi:10.1093/nass/nrn038 · Cited by 32 · see citing works
Methylthioadenosine and polyamine biosynthesis in a Saccharomyces cerevisiae meu1Δ mutant
Chattopadhyay, M. K., Tabor, C. W., & Tabor, H. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.02.144 · Cited by 20 · see citing works
Fernández‐Irigoyen, J., Santamaría, M., Sánchez‐Quiles, V., Latasa, M. U., Santamaría, E., Muñoz, J., del Pino, M. M. S., Valero, M. L., Prìeto, J., Avila, M. A., et al. (2008) · Biochemical Journal · doi:10.1042/bj20071569 · Cited by 17 · see citing works
Nicotinamide riboside phosphorylase from beef liver: Purification and characterization
Imai, T., & Anderson, B. M. (1987) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(87)90101-9 · Cited by 7 · see citing works
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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 · see citing works
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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
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Stein, L. R., & Imai, S. (2012) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2012.06.005 · Cited by 529 · see citing works
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Ratajczak, J., Joffraud, M., Trammell, S. A. J., Ras, R., Canela, N., Boutant, M., Kulkarni, S. S., Rodrigues, M., Redpath, P., Migaud, M. E., et al. (2016) · Nature Communications · doi:10.1038/ncomms13103 · Cited by 378 · see citing works
Self-citationNicotinamide Riboside Preserves Cardiac Function in a Mouse Model of Dilated Cardiomyopathy
Diguet, N., Trammell, S. A. J., Tannous, C., Deloux, R., Piquereau, J., Mougenot, N., Gouge, A., Gressette, M., Manoury, B., Blanc, J., et al. (2018) · Circulation · doi:10.1161/circulationaha.116.026099 · Cited by 358 · see citing works
Self-citationPathways 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
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Gazzaniga, F., Stebbins, R., Chang, S. Z., McPeek, M. A., & Brenner, C. (2009) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00042-08 · Cited by 230 · see citing works
Self-citationThe human NAD metabolome: Functions, metabolism and compartmentalization
Nikiforov, A. A., Kulikova, V., & Ziegler, M. (2015) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2015.1028612 · Cited by 214 · see citing works
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Trammell, S. A. J., & Brenner, C. (2013) · Computational and Structural Biotechnology Journal · doi:10.5936/csbj.201301012 · Cited by 193 · see citing works
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Bradshaw, P. C. (2019) · Nutrients · doi:10.3390/nu11030504 · Cited by 178 · see citing works
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Satoh, A., Stein, L. R., & Imai, S. (2011) · Handbook of experimental pharmacology · doi:10.1007/978-3-642-21631-2_7 · Cited by 171 · see citing works
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Yusri, K., Jose, S., Vermeulen, K. S., Tan, T. C. M., & Sorrentino, V. (2025) · npj Metabolic Health and Disease · doi:10.1038/s44324-025-00067-0 · Cited by 171 · see citing works
Kelly, G. S. (2010) · PubMed · Cited by 135 · see citing works
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
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Klimova, N., Fearnow, A. D., Long, A. N., & Kristián, T. (2019) · Experimental Neurology · doi:10.1016/j.expneurol.2019.113144 · Cited by 106 · see citing works
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Nicotinamide mononucleotide alters mitochondrial dynamics by SIRT3‐dependent mechanism in male mice
Klimova, N., Long, A. N., & Kristián, T. (2019) · Journal of Neuroscience Research · doi:10.1002/jnr.24397 · Cited by 97 · see citing works
Angeletti, C., Amici, A., Gilley, J., Loreto, A., Trapanotto, A. G., Antoniou, C., Merlini, E., Coleman, M. P., & Orsomando, G. (2022) · iScience · doi:10.1016/j.isci.2022.103812 · Cited by 95 · see citing works
Garavaglia, S., Bruzzone, S., Cassani, C., Canella, L., Allegrone, G., Sturla, L., Mannino, E., Millo, E., De Flora, A., & Rizzi, M. (2012) · Biochemical Journal · doi:10.1042/bj20111263 · Cited by 94 · see citing works
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Csiszár, A., Tarantini, S., Yabluchanskiy, A., Balasubramanian, P., Kiss, T., Farkas, E., Baur, J. A., & Ungvari, Z. I. (2019) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00039.2019 · Cited by 93 · see citing works
Evans, C., Bogan, K. L., Song, P., Burant, C. F., Kennedy, R. T., & Brenner, C. (2010) · BMC Chemical Biology · doi:10.1186/1472-6769-10-2 · Cited by 81 · see citing works
Self-citationNicotinamide 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 · see citing works
Lu, S.-P., Kato, M., & Lin, S.-J. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.004010 · Cited by 75 · see citing works
The purinergic neurotransmitter revisited: A single substance or multiple players?
Mutafova–Yambolieva, V. N., & Durnin, L. (2014) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2014.05.012 · Cited by 75 · see citing works
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 · see citing works
Goody, M. F., Kelly, M. W., Lessard, K. N., Khalil, A., & Henry, C. A. (2010) · Developmental Biology · doi:10.1016/j.ydbio.2010.05.513 · Cited by 70 · see citing works
Bogan, K. L., Evans, C., Belenky, P., Song, P., Burant, C. F., Kennedy, R., & Brenner, C. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.056689 · Cited by 63 · see citing works
Self-citationBlack, W. B., Aspacio, D., Bever, D., King, E. J., Zhang, L., & Li, H. (2020) · Microbial Cell Factories · doi:10.1186/s12934-020-01415-z · Cited by 67 · see citing works
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de Figueiredo, L. F., Gossmann, T. I., Ziegler, M., & Schuster, S. (2011) · Biochemical Journal · doi:10.1042/bj20110320 · Cited by 65 · see citing works
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Krypotou, E., Evangelidis, T., Bobonis, J., Pittis, A. A., Gabaldón, T., Scazzocchio, C., Mikros, E., & Diallinas, G. (2015) · Molecular Microbiology · doi:10.1111/mmi.12982 · Cited by 61 · see citing works
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Ohashi, K., Chaleckis, R., Takaine, M., Wheelock, C. E., & Yoshida, S. (2017) · Scientific Reports · doi:10.1038/s41598-017-12392-6 · Cited by 50 · see citing works
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Kristián, T., Balan, I. S., Schuh, R. A., & Onken, M. (2011) · Journal of Neuroscience Research · doi:10.1002/jnr.22626 · Cited by 47 · see citing works
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Zamporlini, F., Ruggieri, S., Mazzola, F., Amici, A., Orsomando, G., & Raffaelli, N. (2014) · FEBS Journal · doi:10.1111/febs.13050 · Cited by 48 · see citing works
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Belenky, P. A., Stebbins, R. C., Bogan, K. L., Evans, C. R., & Brenner, C. (2011) · PLoS ONE · doi:10.1371/journal.pone.0019710 · Cited by 43 · see citing works
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Yaku, K., Palikhe, S., Iqbal, T., Hayat, F., Watanabe, Y., Fujisaka, S., Izumi, H., Yoshida, T., Karim, M., Uchida, H., et al. (2025) · Science Advances · doi:10.1126/sciadv.adr1538 · Cited by 40 · see citing works
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NAD Metabolome Analysis in Human Cells Using 1H NMR Spectroscopy
Shabalin, K. A., Nerinovski, K., Yakimov, A. P., Kulikova, V., Svetlova, M., Solovjeva, L., Khodorkovskiy, M., Gambaryan, S. P., Cunningham, R., Migaud, M. E., et al. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19123906 · Cited by 37 · see citing works
Goody, M. F., Carter, E. V., Kilroy, E. A., Maves, L., & Henry, C. A. (2016) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/bs.ctdb.2016.11.002 · Cited by 34 · see citing works
Nicotinamide Adenine Dinucleotide: The Redox Sensor in Aging-Related Disorders
Schiuma, G., Lara, D., Clement, J. P., Narducci, M., & Rizzo, R. (2024) · Antioxidants and Redox Signaling · doi:10.1089/ars.2023.0375 · Cited by 33 · see citing works
NAD+ precursor supplementation in human ageing: clinical evidence and challenges
Vinten, K. T., Trętowicz, M. M., Coskun, E., van Weeghel, M., Cantó, C., Perez, R. Z., Janssens, G. E., & Houtkooper, R. H. (2025) · Nature Metabolism · doi:10.1038/s42255-025-01387-7 · Cited by 32 · see citing works
Dong, W.-R., Sun, C.-C., Zhu, G., Hu, S.-H., Xiang, L., & Shao, J. (2014) · BMC Microbiology · doi:10.1186/1471-2180-14-29 · Cited by 30 · see citing works
Nicotinamide: A Multifaceted Molecule in Skin Health and Beyond
Camillo, L., Zavattaro, E., & Savoia, P. (2025) · Medicina · doi:10.3390/medicina61020254 · Cited by 32 · see citing works
A pre-steady state and steady state kinetic analysis of the N-ribosyl hydrolase activity of hCD157
Preugschat, F., Carter, L. H., Boros, E. E., Porter, D. J. T., Stewart, E. L., & Shewchuk, L. M. (2014) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2014.09.008 · Cited by 29 · see citing works
Inhibitors of NAD+ Production in Cancer Treatment: State of the Art and Perspectives
Ghanem, M. S., Caffa, I., Monacelli, F., & Nencioni, A. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25042092 · Cited by 28 · see citing works
Purine nucleoside phosphorylase controls nicotinamide riboside metabolism in mammalian cells
Kropotov, A., Kulikova, V., Solovjeva, L., Yakimov, A. P., Nerinovski, K., Svetlova, M., Sudnitsyna, J. S., Plusnina, A., Antipova, M., Khodorkovskiy, M., et al. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102615 · Cited by 29 · see citing works
Biosynthesis of Nicotinamide Mononucleotide: Synthesis Method, Enzyme, and Biocatalytic System
Cheng, F., Li, K.-X., Wu, S., Liu, H., Li, H., Shen, Q., Xue, Y., & Zheng, Y. (2024) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.3c09217 · Cited by 26 · see citing works
NAD+ Metabolism and Interventions in Premature Renal Aging and Chronic Kidney Disease
Chanvillard, L., Tammaro, A., & Sorrentino, V. (2022) · Cells · doi:10.3390/cells12010021 · Cited by 25 · see citing works
Mahor, D., Priyanka, A., Prasad, G. S., & Thakur, K. G. (2016) · PLoS ONE · doi:10.1371/journal.pone.0164279 · Cited by 25 · see citing works
Biochemical and Mutational Analysis of a Novel Nicotinamidase from Oceanobacillus iheyensis HTE831
Sánchez-Carrón, G., García-García, M. I., Perez, R. Z., Takami, H., García‐Carmona, F., & Sánchez‐Ferrer, Á. (2013) · PLoS ONE · doi:10.1371/journal.pone.0056727 · Cited by 19 · see citing works
Nicotinic acid riboside maintains NAD+ homeostasis and ameliorates aging-associated NAD+ decline
Song, W.-S., Shen, X., Du, K., Ramirez, C. B., Park, S. H., Cao, Y., Le, J., Bae, H., Kim, J., Chun, Y., et al. (2025) · Cell Metabolism · doi:10.1016/j.cmet.2025.04.007 · Cited by 17 · see citing works
Dei, M., Vigentini, I., Vitalini, S., Laganaro, A., Iriti, M., Paroni, R. C., & Foschino, R. C. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22010472 · Cited by 17 · see citing works
Gaudino, F., Manfredonia, I., Managò, A., Audrito, V., Raffaelli, N., Vaisitti, T., & Deaglio, S. (2019) · Antioxidants and Redox Signaling · doi:10.1089/ars.2019.7799 · Cited by 16 · see citing works
Carpi, F. M., Cortese, M., Orsomando, G., Polzonetti, V., Vincenzetti, S., Moreschini, B., Coleman, M. P., Magni, G., & Pucciarelli, S. (2018) · Separation Science Plus · doi:10.1002/sscp.201700024 · Cited by 16 · see citing works
Ren, C., Shuang, Z., Chen, Y., Deng, K., Kuang, M., Gong, Z., Zhang, K., Wang, P., Huang, P., Zhou, Z., et al. (2024) · The FASEB Journal · doi:10.1096/fj.202400453r · Cited by 14 · see citing works
Shi, X., Zhang, X., Shi, D., Zhang, X., Li, W., & Tang, J. (2019) · Scientific Reports · doi:10.1038/s41598-018-36446-5 · Cited by 14 · see citing works
Sirtuins in Aging and Age-Related Diseases
Haigis, M. C., & Sinclair, D. A. (2010) · Elsevier eBooks · doi:10.1016/b978-0-12-378638-8.00011-7 · Cited by 13 · see citing works
Risks and rewards of targeting NAD+ homeostasis in the brain
Li, C., & Wu, L. E. (2021) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2021.111545 · Cited by 13 · see citing works
Metabolism and Receptor Mechanisms of Niacin Action
Boronovskiy, S. E., Сергеевна, К. В., & Nartsissov, Y. R. (2024) · Cell and Tissue Biology · doi:10.1134/s1990519x23700025 · Cited by 11 · see citing works
Garau, G., Muzzolini, L., Tornaghi, P., & Degano, M. (2010) · BMC Structural Biology · doi:10.1186/1472-6807-10-14 · Cited by 10 · see citing works
Quantification of Protein Copy Number in Yeast: The NAD+ Metabolome
Mei, S.-C., & Brenner, C. (2014) · PLoS ONE · doi:10.1371/journal.pone.0106496 · Cited by 10 · see citing works
Self-citationStructure, Oligomerization and Activity Modulation in N-Ribohydrolases
Degano, M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23052576 · Cited by 10 · see citing works
The Evolutionary Portrait of Metazoan NAD Salvage
Carneiro, J., Duarte-Pereira, S., Azevedo, L., Castro, L. F. C., Aguiar, P., Moreira, I. S., Amorim, A., & Silva, R. M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0064674 · Cited by 9 · see citing works
CD38 mediates nicotinamide mononucleotide base exchange to yield nicotinic acid mononucleotide
Madawala, R. J., Banks, J. L., Hancock, S. E., Quek, L., Turner, N. A., & Wu, L. E. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.108248 · Cited by 8 · see citing works
Minici, C., Cacciapuoti, G., Leo, E. D., Porcelli, M., & Degano, M. (2012) · Biochemistry · doi:10.1021/bi300209g · Cited by 8 · see citing works
An overview of engineering microbial production of nicotinamide mononucleotide
Li, B., Meng, X., & Liu, W. (2024) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2024.10.014 · Cited by 7 · see citing works
Nicotinamide riboside–amino acid conjugates that are stable to purine nucleoside phosphorylase
Hayat, F., & Migaud, M. E. (2020) · Organic & Biomolecular Chemistry · doi:10.1039/d0ob00134a · Cited by 7 · see citing works
Singh, R. K., Steyaert, J., & Versées, W. (2017) · Protein Science · doi:10.1002/pro.3141 · Cited by 7 · see citing works
Wohlgemuth, R. (2024) · Life · doi:10.3390/life14030364 · Cited by 3 · see citing works
Carriles, A. A., Muzzolini, L., Minici, C., Tornaghi, P., Patrone, M., & Degano, M. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25137032 · Cited by 1 · see citing works
The NARly side of whole-body NAD homeostasis
Brenner, C. (2025) · Cell Metabolism · doi:10.1016/j.cmet.2025.06.003 · Cited by 1 · see citing works
Self-citationCancer, Senescence, and Aging: Translation from Basic Research to Clinics
LLeonart, M. E., Carnero, A., Paciucci, R., Wang, Z., & Shomron, N. (2011) · Journal of Aging Research · doi:10.4061/2011/692301 · Cited by 1 · see citing works
Patrone, M., Galasyn, G. S., Kerin, F., Nyitray, M. M., Parkin, D. W., Stockman, B. J., & Degano, M. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105077 · Cited by 1 · see citing works
Novel NAD+ metabolomic technologies and their applications to Nicotinamide Riboside interventions
Trammell, S. A. J., Wright, M. E., Piper, R. C., Brenner, C., Slusarski, D. C., & Wilson, M. E. (2016) · doi:10.17077/etd.mk206led · Cited by 1 · see citing works
Self-citationBalarezo-Cisneros, L. N. (2020)
Cell-matrix adhesion in muscle development and disease
Goody, M. F. (2012) · DigitalCommons (California Polytechnic State University)
Metabolism and Receptor Mechanisms of Niacin Action
Boronovskiy, S. E., Сергеевна, К. В., & Nartsissov, Y. R. (2023) · Tsitologiya · doi:10.31857/s0041377123060032
Panda, N. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.10.05.680515
Hao, T., Liu, R., Tang, Z., Li, Y., Qu, W., Luo, W., Gui, L., Zhu, P., & Zhang, B. (2025) · Industrial Crops and Products · doi:10.1016/j.indcrop.2025.122186
Sun, T., Yang, Y., Xie, J., Rao, Z., Han, R., & Cao, L. (2026) · Synthetic and Systems Biotechnology · doi:10.1016/j.synbio.2026.03.016
- Authors
- Belenky, P., Christensen, K. C., Gazzaniga, F., Pletnev, A. A., & Brenner, C.
- Affiliations
- Dartmouth–Hitchcock Medical Center (US)
- Corresponding author
- Brenner, Charles
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2009-01
- Volume
- 284
- Issue
- 1
- Pages
- 158-164
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC2610512
- OpenAlex
- W2039774617
- Cited by
- 95
- References
- 43
- Citations by year
- 2026: 1 · 2025: 10 · 2024: 9 · 2023: 5 · 2022: 6 · 2021: 3 · 2020: 4 · 2019: 7 · 2018: 4 · 2017: 6 · 2016: 5 · 2015: 3 · 2014: 6 · 2013: 3 · 2012: 3
- FWCI
- 2.71
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of General Medical Sciences (T32GM008704)
- 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
- Health Sciences › Medicine › Rheumatology › Folate and B Vitamins Research
- Keywords
- nicotinamide riboside, purine nucleoside phosphorylase, MTAP, Sir2, replicative lifespan, gene silencing, sirtuins, yeast, mammals
- MeSH terms
- Histone Deacetylases, Humans, NAD, Niacinamide, Purine-Nucleoside Phosphorylase, Saccharomyces cerevisiae, Phosphotransferases (Alcohol Group Acceptor), Sirtuins, Silent Information Regulator Proteins, Saccharomyces cerevisiae, Sirtuin 2
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