The DOI matches its Crossref record; 75 of the 76 references it cites were found in a registry or an index.
Microbial NAD Metabolism: Lessons from Comparative Genomics
Open accessAbstract
SUMMARY: NAD is a coenzyme for redox reactions and a substrate of NAD-consuming enzymes, including ADP-ribose transferases, Sir2-related protein lysine deacetylases, and bacterial DNA ligases. Microorganisms that synthesize NAD from as few as one to as many as five of the six identified biosynthetic precursors have been identified. De novo NAD synthesis from aspartate or tryptophan is neither universal nor strictly aerobic. Salvage NAD synthesis from nicotinamide, nicotinic acid, nicotinamide riboside, and nicotinic acid riboside occurs via modules of different genes. Nicotinamide salvage genes nadV and pncA , found in distinct bacteria, appear to have spread throughout the tree of life via horizontal gene transfer. Biochemical, genetic, and genomic analyses have advanced to the point at which the precursors and pathways utilized by a microorganism can be predicted. Challenges remain in dissecting regulation of pathways.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The cited source says what the claim attributes to it.
In the citing paper
“However, mammals do not have a homologous enzyme (12, 25–28).”
From Nicotinamide riboside and nicotinamide mononucleotide facilitate NAD + synthesis via enterohepatic circulation (2025) · cites this paper as [25]
The cited source says what the claim attributes to it.
In the citing paper
“Most bacteria have a NAM deamidase, an enzyme that converts NAM into NA.”
From Nicotinamide riboside and nicotinamide mononucleotide facilitate NAD + synthesis via enterohepatic circulation (2025) · cites this paper as [25]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
MrBayes 3: Bayesian phylogenetic inference under mixed models
Ronquist, F., & Huelsenbeck, J. P. (2003) · Bioinformatics · doi:10.1093/bioinformatics/btg180 · Cited by 29,194
Whole-Genome Random Sequencing and Assembly of Haemophilus influenzae Rd
Fleischmann, R. D., Adams, M. D., White, O. R., Clayton, R. A., Kirkness, E. F., Kerlavage, A. R., Bult, C. J., Tomb, J.-F., Dougherty, B. A., Merrick, J. M., et al. (1995) · Science · doi:10.1126/science.7542800 · Cited by 5,731
Environmental genome shotgun sequencing of the sargasso sea
Venter, J. C., Remington, K., Heidelberg, J. F., Halpern, A. L., Rusch, D., Eisen, J. A., Wu, D., Paulsen, I., Nelson, K. E., Nelson, W., et al. (2004) · Science · doi:10.1126/science.1093857 · Cited by 4,376
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
Bayesian Inference of Phylogeny and Its Impact on Evolutionary Biology
Huelsenbeck, J. P., Ronquist, F., Nielsen, R., & Bollback, J. P. (2001) · Science · doi:10.1126/science.1065889 · Cited by 2,737
Genes required for mycobacterial growth defined by high density mutagenesis
Sassetti, C. M., Boyd, D. H., & Rubin, E. J. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03425.x · Cited by 2,544
The Subsystems Approach to Genome Annotation and its Use in the Project to Annotate 1000 Genomes
Overbeek, R. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki866 · Cited by 2,040
Toward Automatic Reconstruction of a Highly Resolved Tree of Life
Ciccarelli, F. D., Doerks, T., von Mering, C., Creevey, C. J., Snel, B., & Bork, P. (2006) · Science · doi:10.1126/science.1123061 · Cited by 1,663
Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins
Frye, R. A. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3000 · Cited by 1,409
Benson, D. A. (2004) · Nucleic Acids Research · doi:10.1093/nar/gki063 · Cited by 1,020
Cited by
Sorted by citations
Systematic genome assessment of B-vitamin biosynthesis suggests co-operation among gut microbes
Magnúsdóttir, S., Ravcheev, D., de Crécy-Lagard, V., & Thiele, I. (2015) · Frontiers in Genetics · doi:10.3389/fgene.2015.00148 · Cited by 876
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
Self-citationMetabolism of Dietary and Microbial Vitamin B Family in the Regulation of Host Immunity
Yoshii, K., Hosomi, K., Sawane, K., & Kunisawa, J. (2019) · Frontiers in Nutrition · doi:10.3389/fnut.2019.00048 · Cited by 607
It takes two to tango: NAD(+) and sirtuins in aging/longevity control
Imai, S.-I., & Guarente, L. (2016) · npj Aging and Mechanisms of Disease · doi:10.1038/npjamd.2016.17 · Cited by 394
NADPH-generating systems in bacteria and archaea
Spaans, S. K., Weusthuis, R. A., John van der, O. O. S. T., & Kengen, S. W. M. (2015) · Frontiers in Microbiology · doi:10.3389/fmicb.2015.00742 · Cited by 389
Vitamins, the gut microbiome and gastrointestinal health in humans
Pham, V. T., Dold, S., Rehman, A., Bird, J. K., & Steinert, R. E. (2021) · Nutrition Research · doi:10.1016/j.nutres.2021.09.001 · Cited by 300
Biological Properties of Vitamins of the B-Complex, Part 1: Vitamins B1, B2, B3, and B5
Hrubša, M., Siatka, T., Najmanová, I., Vopršalová, M., Krčmová, L. K., Matoušová, K., Javorská, L., Macáková, K., Mercolini, L., Remião, F., et al. (2022) · Nutrients · doi:10.3390/nu14030484 · Cited by 284
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
Li, F., Li, Y., Cao, Y., Wang, L., Liu, C., Shi, L., & Song, H. (2018) · Nature Communications · doi:10.1038/s41467-018-05995-8 · Cited by 233
Nicotinamide Riboside—The Current State of Research and Therapeutic Uses
Mehmel, M., Jovanović, N. D., & Spitz, U. P. (2020) · Nutrients · doi:10.3390/nu12061616 · Cited by 231
Challenging microalgal vitamins for human health
Del Mondo, A., Smerilli, A., Sané, E., Sansone, C., & Brunet, C. (2020) · Microbial Cell Factories · doi:10.1186/s12934-020-01459-1 · Cited by 220
Functional Roles of B‐Vitamins in the Gut and Gut Microbiome
Uebanso, T., Shimohata, T., Mawatari, K., & Takahashi, A. (2020) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.202000426 · Cited by 234
Round, round we go – strategies for enzymatic cofactor regeneration
Mordhorst, S., & Andexer, J. N. (2020) · Natural Product Reports · doi:10.1039/d0np00004c · Cited by 216
B Vitamins and Their Roles in Gut Health
Hossain, K. S., Amarasena, S., & Mayengbam, S. (2022) · Microorganisms · doi:10.3390/microorganisms10061168 · Cited by 200
The role of NAD+ metabolism and its modulation of mitochondria in aging and disease
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 194
NAD precursors cycle between host tissues and the gut microbiome
Chellappa, K., McReynolds, M. R., Lu, W., Zeng, X., Makarov, M., Hayat, F., Mukherjee, S., Bhat, Y. R., Lingala, S. R., Shima, R. T., et al. (2022) · Cell Metabolism · doi:10.1016/j.cmet.2022.11.004 · Cited by 146
Engineering a nicotinamide mononucleotide redox cofactor system for biocatalysis
Black, W. B., Zhang, L., Mak, W. S., Maxel, S., Cui, Y., King, E. J., Fong, B. L., Martinez, A. S., Siegel, J. B., & Li, H. (2019) · Nature Chemical Biology · doi:10.1038/s41589-019-0402-7 · Cited by 131
Regulation of and challenges in targeting NAD+ metabolism
Migaud, M. E., Ziegler, M., & Baur, J. A. (2024) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-024-00752-w · Cited by 142
The Natural History of ADP-Ribosyltransferases and the ADP-Ribosylation System
Aravind, L., Zhang, D., de Souza, R. F., Anand, S., & Iyer, L. M. (2014) · Current topics in microbiology and immunology · doi:10.1007/82_2014_414 · Cited by 142
Casting light on Asgardarchaeota metabolism in a sunlit microoxic niche
Bulzu, P., Andrei, A., Salcher, M. M., Mehrshad, M., Inoue, K., Kandori, H., Béjà, O., Ghai, R., & Banciu, H. L. (2019) · Nature Microbiology · doi:10.1038/s41564-019-0404-y · Cited by 129
Li, F., Li, Y., Sun, L., Chen, X., An, X., Yin, C., Cao, Y., Wu, H. C., & Song, H. (2018) · ACS Synthetic Biology · doi:10.1021/acssynbio.7b00390 · Cited by 115
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
Self-citationThe chemistry of the vitamin B3 metabolome
Makarov, M. V., Trammell, S. A. J., & Migaud, M. E. (2018) · Biochemical Society Transactions · doi:10.1042/bst20180420 · Cited by 115
Fangmann, D., Theismann, E., Türk, K., Schulte, D. M., Relling, I., Hartmann, K., Keppler, J. K., Knipp, J.-R., Rehman, A., Heinsen, F., et al. (2017) · Diabetes Care · doi:10.2337/dc17-1967 · Cited by 104
Self-citationAlegre, G. F. S., & Pastore, G. M. (2023) · Current Nutrition Reports · doi:10.1007/s13668-023-00475-y · Cited by 101
NMNAT Expression and its Relation to NAD Metabolism
Jayaram, H. N., Kusumanchi, P., & Yalowitz, J. A. (2011) · Current Medicinal Chemistry · doi:10.2174/092986711795590138 · Cited by 92
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
Self-citationBurroughs, A. M., & Aravind, L. (2020) · Journal of Bacteriology · doi:10.1128/jb.00365-20 · Cited by 78
Pharmacokinetics of isoniazid: The good, the bad, and the alternatives
Erwin, E. R., Addison, A. P., John, S. F., Olaleye, O. A., & Rosell, R. C. (2019) · Tuberculosis · doi:10.1016/j.tube.2019.04.012 · Cited by 78
Diversity of membrane transport proteins for vitamins in bacteria and archaea
Jaehme, M., & Slotboom, D. J. (2014) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2014.05.006 · Cited by 74
β-nicotinamide mononucleotide (NMN) production in Escherichia coli
Marinescu, G. C., Popescu, R. G., Stoian, G., & Dinischiotu, A. (2018) · Scientific Reports · doi:10.1038/s41598-018-30792-0 · Cited by 71
de Souza, R. F., & Aravind, L. (2012) · Molecular BioSystems · doi:10.1039/c2mb05487f · Cited by 66
Nutrient salvaging and metabolism by the intracellular pathogen Legionella pneumophila
Fonseca, M. V., & Swanson, M. S. (2014) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2014.00012 · Cited by 69
Dehydrogenases of acetic acid bacteria
Qin, Z., Yu, S., Chen, J., & Zhou, J. (2021) · Biotechnology Advances · doi:10.1016/j.biotechadv.2021.107863 · Cited by 66
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
Self-citationGaleazzi, L., Bocci, P., Amici, A., Brunetti, L., Ruggieri, S., Romine, M., Reed, S., Osterman, A. L., Rodionov, D. A., Sorci, L., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.275818 · Cited by 67
Identification of evolutionary and kinetic drivers of NAD-dependent signaling
Bockwoldt, M., Houry, D., Niere, M., Gossmann, T. I., Reinartz, I., Schug, A. H., Ziegler, M., & Heiland, I. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1902346116 · Cited by 68
Black, 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
Phages reconstitute NAD+ to counter bacterial immunity
Osterman, I. А., Samra, H., Rousset, F., Loseva, E., Itkin, M., Malitsky, S., Yirmiya, E., Millman, A., & Sorek, R. (2024) · Nature · doi:10.1038/s41586-024-07986-w · Cited by 66
Origins of Life: The Primal Self-Organization
Egel, R., Mulkidjanian, A. Y., & Lankenau, D. (2011) · Springer eBooks · doi:10.1007/978-3-642-21625-1 · Cited by 66
Pathway analysis of NAD+ metabolism
de Figueiredo, L. F., Gossmann, T. I., Ziegler, M., & Schuster, S. (2011) · Biochemical Journal · doi:10.1042/bj20110320 · Cited by 69
Photoelectric Bacteria Enhance the In Situ Production of Tetrodotoxin for Antitumor Therapy
Wang, X., Niu, M., Fan, J., Chen, Q., & Zhang, X. (2021) · Nano Letters · doi:10.1021/acs.nanolett.1c00408 · Cited by 62
Borrelia burgdorferi : Carbon Metabolism and the Tick-Mammal Enzootic Cycle
Corona, A., & Schwartz, I. S. (2015) · Microbiology Spectrum · doi:10.1128/microbiolspec.mbp-0011-2014 · Cited by 62
Metabolic modeling reveals a multi-level deregulation of host-microbiome metabolic networks in IBD
Taubenheim, J., Kadibalban, A. S., Zimmermann, J., Taubenheim, C., Tran, F., Schreiber, S., Rosenstiel, P. C., Aden, K., & Kaleta, C. (2025) · Nature Communications · doi:10.1038/s41467-025-60233-2 · Cited by 64
Liu, Y., Yasawong, M., & Yu, B. (2021) · Microbial Biotechnology · doi:10.1111/1751-7915.13901 · Cited by 57
Essential Amino Acid Metabolites as Chemical Mediators of Host-Microbe Interaction in the Gut
McCann, J. R., & Rawls, J. F. (2023) · Annual Review of Microbiology · doi:10.1146/annurev-micro-032421-111819 · Cited by 64
Desguin, B., Soumillion, P., Pascal Hols, A., & Hausinger, R. P. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1600486113 · Cited by 57
Age-Dependent Decline of NAD+—Universal Truth or Confounded Consensus?
Peluso, A. A., Damgaard, M. V., Mori, M. A., & Treebak, J. T. (2021) · Nutrients · doi:10.3390/nu14010101 · Cited by 61
Turło, J., Gajzlerska-Majewska, W., Klimaszewska, M., Król, M., Dawidowski, M., & Gutkowska, B. (2012) · Enzyme and Microbial Technology · doi:10.1016/j.enzmictec.2012.08.008 · Cited by 53
NAD+ biosynthesis and salvage – a phylogenetic perspective
Gossmann, T. I., Ziegler, M., Puntervoll, P., de Figueiredo, L. F., Schuster, S., & Heiland, I. (2012) · FEBS Journal · doi:10.1111/j.1742-4658.2012.08559.x · Cited by 52
Improving the production of NAD+ via multi-strategy metabolic engineering in Escherichia coli
Yang, L., Mu, X., Nie, Y., & Xu, Y. (2021) · Metabolic Engineering · doi:10.1016/j.ymben.2021.01.012 · Cited by 50
Vibrio Phage KVP40 Encodes a Functional NAD + Salvage Pathway
Lee, J. Y., Li, Z., & Miller, E. S. (2017) · Journal of Bacteriology · doi:10.1128/jb.00855-16 · Cited by 49
Genomics-driven Reconstruction of Acinetobacter NAD Metabolism
Sorci, L., Blaby, I. K., Ingeniis, J. D., Gerdes, S., Raffaelli, N., de Crécy‐Lagard, V., & Osterman, A. L. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.185629 · Cited by 48
Zamporlini, F., Ruggieri, S., Mazzola, F., Amici, A., Orsomando, G., & Raffaelli, N. (2014) · FEBS Journal · doi:10.1111/febs.13050 · Cited by 48
Mahapatra, S., Woolhiser, L. K., Lenaerts, A. J. M., Johnson, J. L., Eisenach, K. D., Joloba, M. L., Boom, W. H., & Belisle, J. T. (2011) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.05486-11 · Cited by 47
In vitro metabolic engineering for the salvage synthesis of NAD
Honda, K., Hara, N., Cheng, M., Nakamura, A., Mandai, K., Okano, K., & Ohtake, H. (2016) · Metabolic Engineering · doi:10.1016/j.ymben.2016.02.005 · Cited by 45
Ren, Z., Xu, Y., Li, T., Sun, W., Tang, Z., Wang, Y., Zhou, K., Li, J., Ding, Q., Liang, K., et al. (2022) · Animal Nutrition · doi:10.1016/j.aninu.2022.06.009 · Cited by 44
Nicotinamide Adenine Dinucleotide in Aging Biology: Potential Applications and Many Unknowns
Bhasin, S., Seals, D. R., Migaud, M. E., Musi, N., & Baur, J. A. (2023) · Endocrine Reviews · doi:10.1210/endrev/bnad019 · Cited by 50
Comparative genomics of NAD(P) biosynthesis and novel antibiotic drug targets
Bi, J., Wang, H., & Xie, J. (2010) · Journal of Cellular Physiology · doi:10.1002/jcp.22419 · Cited by 43
Dual control of NAD+ synthesis by purine metabolites in yeast
Pinson, B., Ceschin, J., Saint‐Marc, C., & Daignan‐Fornier, B. (2019) · eLife · doi:10.7554/elife.43808 · Cited by 43
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
“However, mammals do not have a homologous enzyme ( 12 , 25 – 28 ).”
Sun, X., Dey, P., Bruno, R. S., & Zhu, J. (2022) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2022.109094 · Cited by 41
Lai, K.-K., Davis‐Richardson, A. G., Dias, R., & Triplett, E. W. (2016) · Frontiers in Microbiology · doi:10.3389/fmicb.2016.00547 · Cited by 40
The emergence of the nicotinamide riboside kinases in the regulation of NAD+ metabolism
Fletcher, R. S., & Lavery, G. G. (2018) · Journal of Molecular Endocrinology · doi:10.1530/jme-18-0085 · Cited by 40
Evidence that the nadA motif is a bacterial riboswitch for the ubiquitous enzyme cofactor NAD+
Malkowski, S. N., Spencer, T. C. J., & Breaker, R. R. (2019) · RNA · doi:10.1261/rna.072538.119 · Cited by 39
Discovery and Characterization of Novel Nonsubstrate and Substrate NAMPT Inhibitors
Wilsbacher, J. L., Cheng, M., Cheng, D., Trammell, S. A. J., Shi, Y., Guo, J. Q., Koeniger, S. L., Kovar, P. J., He, Y., Selvaraju, S., et al. (2017) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-16-0819 · Cited by 38
Self-citationBiosynthesis of NAD and Its Manipulation in Plants☆
Noctor, G., Hager, J., & Li, S. (2011) · Advances in botanical research · doi:10.1016/b978-0-12-386479-6.00002-0 · Cited by 38
Current Uncertainties and Future Challenges Regarding NAD+ Boosting Strategies
Poljšak, B., Kovač, V., & Milisav, I. (2022) · Antioxidants · doi:10.3390/antiox11091637 · Cited by 42
On the evolution of coenzyme biosynthesis
Kirschning, A. (2022) · Natural Product Reports · doi:10.1039/d2np00037g · Cited by 37
Anaerobic degradation of aromatic amino acids by the hyperthermophilic archaeon Ferroglobus placidus
Aklujkar, M., Risso, C., Smith, J. A., Beaulieu, D., Dubay, R., Giloteaux, L., DiBurro, K., & Holmes, D. E. (2014) · Microbiology · doi:10.1099/mic.0.083261-0 · Cited by 37
Quinolinate Salvage and Insights for Targeting NAD Biosynthesis in Group A Streptococci
Sorci, L., Blaby, I. K., Rodionova, I. A., Ingeniis, J. D., Tkachenko, S., de Crécy‐Lagard, V., & Osterman, A. L. (2012) · Journal of Bacteriology · doi:10.1128/jb.02002-12 · Cited by 35
Ott, E., Kawaguchi, Y., Gutmann-Özgen, N., Yamagishi, A., Rabbow, E., Rettberg, P., Weckwerth, W., & Milojević, T. (2019) · Frontiers in Microbiology · doi:10.3389/fmicb.2019.00909 · Cited by 35
Observing 3-hydroxyanthranilate-3,4-dioxygenase in action through a crystalline lens
Wang, Y., Liu, K. F., Yang, Y., Davis, I., & Liu, A. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2005327117 · Cited by 35
Structure and ligand binding of the ADP-binding domain of the NAD+ riboswitch
Huang, L., Wang, J., & Lilley, D. M. J. (2020) · RNA · doi:10.1261/rna.074898.120 · Cited by 33
From bacteria to biomedicine: Developing therapies exploiting NAD+ metabolism
Chen, Y., Ying, Y., Lalsiamthara, J., Zhao, Y., İmani, S., Li, X., Liu, S., & Wang, Q. (2023) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2023.106974 · Cited by 30
Wu, R., Zhang, F., Liu, L., Li, W., Pichersky, E., & Wang, G. (2018) · Molecular Plant · doi:10.1016/j.molp.2018.07.003 · Cited by 30
Therapeutic potential of nicotinamide adenine dinucleotide (NAD)
Arenas‐Jal, M., Suñé-Negre, J. M., & García‐Montoya, E. (2020) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2020.173158 · Cited by 30
Yamamoto, Y., Nakanishi, Y., Murakami, S., Aw, W., Tsukimi, T., Nozu, R., Ueno, M., Hioki, K., Nakahigashi, K., Hirayama, A., et al. (2018) · Microorganisms · doi:10.3390/microorganisms6040101 · Cited by 30
NAD homeostasis in the bacterial response to DNA/RNA damage
Sorci, L., Ruggieri, S., & Raffaelli, N. (2014) · DNA repair · doi:10.1016/j.dnarep.2014.07.014 · Cited by 29
Energy‐Coupling Factor Transporters as Novel Antimicrobial Targets
Bousis, S., Setyawati, I., Diamanti, E., Slotboom, D. J., & Hirsch, A. K. H. (2018) · Advanced Therapeutics · doi:10.1002/adtp.201800066 · Cited by 28
B Vitamins, Glucoronolactone and the Immune System: Bioavailability, Doses and Efficiency
Munteanu, C., & Schwartz, B. (2023) · Nutrients · doi:10.3390/nu16010024 · Cited by 30
Hypothalamic NAD+-Sirtuin Axis: Function and Regulation
Roh, E., & Kim, M. (2020) · Biomolecules · doi:10.3390/biom10030396 · Cited by 30
Li, Q., Meng, D., & You, C. (2022) · Enzyme and Microbial Technology · doi:10.1016/j.enzmictec.2022.110122 · Cited by 27
Okon, E., Dethlefsen, S., Pel’nikevich, A. D., van Barneveld, A., Munder, A., & Tümmler, B. (2016) · International Journal of Medical Microbiology · doi:10.1016/j.ijmm.2016.09.007 · Cited by 27
Kong, L., Liu, T., Yao, Q., Zhang, X., Xu, W., & Qin, J. (2022) · Journal of the Science of Food and Agriculture · doi:10.1002/jsfa.12253 · Cited by 26
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 28
Prebiotic Synthesis of Aspartate Using Life’s Metabolism as a Guide
Harrison, S. A., Webb, W. L., Rammu, H., & Lane, N. (2023) · Life · doi:10.3390/life13051177 · Cited by 25
A finely tuned regulatory circuit of the nicotinic acid degradation pathway in Pseudomonas putida
Jiménez, J. I., Juárez, J. F., García, J. L., & Dı́az, E. (2011) · Environmental Microbiology · doi:10.1111/j.1462-2920.2011.02471.x · Cited by 25
Gene Transfers Shaped the Evolution of De Novo NAD + Biosynthesis in Eukaryotes
Ternes, C. M., & Schönknecht, G. (2014) · Genome Biology and Evolution · doi:10.1093/gbe/evu185 · Cited by 24
Nicotinamide Riboside-Conditioned Microbiota Deflects High-Fat Diet-Induced Weight Gain in Mice
Lozada-Fernández, V. V., deLeon, O., Kellogg, S. L., Saravia, F. L., Hadiono, M. A., Atkinson, S. N., Grobe, J. L., & Kirby, J. R. (2022) · mSystems · doi:10.1128/msystems.00230-21 · Cited by 23
Teramoto, H., Suda, M., Inui, M., & Yukawa, H. (2010) · Applied and Environmental Microbiology · doi:10.1128/aem.00906-10 · Cited by 23
Skliros, D., Kalatzis, P. G., Katharios, P., & Flemetakis, E. (2016) · Frontiers in Microbiology · doi:10.3389/fmicb.2016.01807 · Cited by 23
Nicotinamide Coenzyme Synthesis: A Case of Ribonucleotide Emergence or a Byproduct of the RNA World?
Raffaelli, N. (2011) · Springer eBooks · doi:10.1007/978-3-642-21625-1_9 · Cited by 23
Vitamin biosynthesis in the gut: interplay between mammalian host and its resident microbiota
Tarracchini, C., Lordan, C., Milani, C., Moreira, L. D. P. D., Alabedallat, Q. M., de LeBlanc, A. D. M., Turroni, F., Lugli, G. A., Mancabelli, L., Longhi, G., et al. (2025) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00184-23 · Cited by 29
The coenzyme/protein pair and the molecular evolution of life
Kirschning, A. (2020) · Natural Product Reports · doi:10.1039/d0np00037j · Cited by 23
Peluso, A. A., Lundgaard, A. T., Babaei, P., Mousovich‐Neto, F., Rocha, A. L. S., Damgaard, M. V., Bak, E. G., Gnanasekaran, T., Dollerup, O. L., Trammell, S. A. J., et al. (2023) · npj Aging · doi:10.1038/s41514-023-00106-4 · Cited by 25
Role of HCA2 in Regulating Intestinal Homeostasis and Suppressing Colon Carcinogenesis
Li, Z., MCCAFFERTY, K. J., & Judd, R. L. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.606384 · Cited by 21
A single regulator NrtR controls bacterial NAD+ homeostasis via its acetylation
Gao, R., Wei, W., Hassan, B. H., Li, J., Deng, J., & Feng, Y. (2019) · eLife · doi:10.7554/elife.51603 · Cited by 21
Rahim, N. A., Zhu, Y., Cheah, S.-E., Johnson, M. D., Yu, H. H., Sidjabat, H. E., Butler, M. S., Cooper, M. A., Fu, J. W., Paterson, D. L., et al. (2021) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.0c00661 · Cited by 21
Shi, Q., Yin, T., Zeng, C., Pan, H., Chen, Z., Wang, L., Wang, B., Zheng, M., & Cai, L. (2024) · Bioactive Materials · doi:10.1016/j.bioactmat.2024.03.032 · Cited by 20
Metadata
- Authors
- Gazzaniga, F., Stebbins, R., Chang, S. Z., McPeek, M. A., & Brenner, C.
- Affiliations
- Dartmouth College (US)
- University of Iowa (US)
- Venue
- Microbiology and Molecular Biology Reviews
- Publisher
- American Society for Microbiology
- Published
- 2009-09
- Volume
- 73
- Issue
- 3
- Pages
- 529-541
- ISSN
- 1092-2172 (ISSN-L)
- 1098-5557
- PMC
- PMC2738131
- OpenAlex
- W2055192452
- Cited by
- 230
- References
- 76
- Citations by year
- 2026: 17 · 2025: 17 · 2024: 19 · 2023: 18 · 2022: 25 · 2021: 14 · 2020: 21 · 2019: 15 · 2018: 16 · 2017: 7 · 2016: 15 · 2015: 5 · 2014: 13 · 2013: 5 · 2012: 6
- FWCI
- 0.59
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Microbiology and Molecular Biology Reviews (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Science Foundation
- Dartmouth College
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Keywords
- NAD+ metabolism, NAD biosynthesis, nicotinamide riboside, horizontal gene transfer, pncA, comparative genomics
- MeSH terms
- Bacteria, NAD, Genome, Bacterial, Sequence Homology, Amino Acid, Evolution, Molecular, Gene Transfer, Horizontal, Genomics, Biosynthetic Pathways
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review