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Microbial NAD Metabolism: Lessons from Comparative Genomics
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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.
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“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]
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“Most bacteria have a NAM deamidase, an enzyme that converts NAM into NA.”
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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 2,019
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
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de Buhr, N., & von Köckritz‐Blickwede, M. (2021) · mBio · doi:10.1128/mbio.03304-20 · Cited by 22
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Gold, D. A., & Sinclair, D. A. (2022) · Molecular Biology and Evolution · doi:10.1093/molbev/msac192 · Cited by 17
Zhou, J., Li, S., Li, H., Jin, Y., Bai, F., Cheng, Z., & Wu, W. (2021) · Microorganisms · doi:10.3390/microorganisms9040753 · Cited by 19
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Zhu, Y., Picard, M.-È., Zhang, Q., Barma, J., Després, X. M., Mei, X., Zhang, L., Duvignaud, J., Couture, M., Zhu, W., et al. (2016) · Chemical Science · doi:10.1039/c6sc00771f · Cited by 18
Olesen, S. V., Rajabi, N., Svensson, B., Olsen, C. A., & Madsen, A. S. (2018) · Biochemistry · doi:10.1021/acs.biochem.8b00306 · Cited by 16
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Han, S.-H., Song, M., & Keum, Y. (2020) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.0c00696 · Cited by 17
Gossmann, T. I., & Ziegler, M. (2014) · DNA repair · doi:10.1016/j.dnarep.2014.07.005 · Cited by 16
Gut microbiota severely hampers the efficacy of NAD-lowering therapy in leukemia
ElMokh, O., Matsumoto, S., Biniecka, P., Bellotti, A., Schaeuble, K., Piacente, F., Gallart‐Ayala, H., Ivanišević, J., Stamenkovic, I., Nencioni, A., et al. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-04763-3 · Cited by 16
Huang, J., Liang, C., Natarajan, M., Barone, P. W., Wolfrum, J. M., Lee, Y. H., Rice, S. A., & Springs, S. L. (2022) · Molecular Therapy — Methods & Clinical Development · doi:10.1016/j.omtm.2022.04.006 · Cited by 16
Esquirol, L., Peat, T. S., Wilding, M., Lucent, D., French, N. G., Hartley, C. J., Newman, J. M., & Scott, C. S. (2018) · PLoS ONE · doi:10.1371/journal.pone.0192736 · Cited by 16
Lu, X., Yang, R., Chen, Y., & Chen, D. (2024) · iScience · doi:10.1016/j.isci.2024.109174 · Cited by 16
Integrated annotation prioritizes metabolites with bioactivity in inflammatory bowel disease
Bhosle, A., Bae, S., Zhang, Y., Chun, E., Ávila-Pacheco, J., Geistlinger, L., Pishchany, G., Glickman, J. N., Michaud, M., Waldron, L., et al. (2024) · Molecular Systems Biology · doi:10.1038/s44320-024-00027-8 · Cited by 16
Cialabrini, L., Ruggieri, S., Kazanov, M. D., Sorci, L., Mazzola, F., Orsomando, G., Osterman, A. L., & Raffaelli, N. (2013) · PLoS ONE · doi:10.1371/journal.pone.0065595 · Cited by 15
Bitew, M. A., Khoo, C. A., Neha, N., Souza, D. P. D., Tull, D., Wawegama, N. K., Newton, H. J., & Sansom, F. M. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.005190 · Cited by 15
Wang, Q., Hassan, B. H., Lou, N., Merritt, J. L., & Feng, Y. (2019) · The FASEB Journal · doi:10.1096/fj.201802179rr · Cited by 15
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
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Brickman, T. J., Suhadolc, R. J., McKelvey, P. J., & Armstrong, S. K. (2016) · Molecular Microbiology · doi:10.1111/mmi.13566 · Cited by 14
Taniguchi, H., Sungwallek, S., Chotchuang, P., Okano, K., & Honda, K. (2017) · Journal of Bacteriology · doi:10.1128/jb.00359-17 · Cited by 14
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Sharma, S. A., Hsieh, Y.-C., Dietze, J., Bockwoldt, M., Strømland, Ø., Ziegler, M., & Heiland, I. (2022) · Metabolites · doi:10.3390/metabo12070569 · Cited by 14
Frederick, D. W., Trefely, S., Buas, A., Goodspeed, J., Singh, J. P., Mesaros, C., Baur, J. A., & Snyder, N. W. (2017) · The Analyst · doi:10.1039/c7an01378g · Cited by 13
Weagley, J. S., Zaydman, M. A., Venkatesh, S., Sasaki, Y., Damaraju, N., Yenkin, A. L., Buchser, W., Rodionov, D. A., Osterman, A. L., Ahmed, T., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.110738 · Cited by 13
Colonic mechanism of serum NAD+ depletion induced by DEHP during pregnancy
Hong, Y. S., Ning, X., Liang, Y.-Y., Li, X., Cui, Y., Wu, W., Cai, Y., Zhao, S., Zhu, M., Zhong, T.-X., et al. (2023) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2023.162188 · Cited by 12
Guragain, M., Jennings‐Gee, J. E., Cattelan, N., Finger, M. E., Conover, M. S., Hollis, T., & Deora, R. (2018) · Journal of Bacteriology · doi:10.1128/jb.00712-17 · Cited by 12
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Ito, T., Totoki, T., Takada, S., Otsuka, S., & Maruyama, I. (2021) · Scientific Reports · doi:10.1038/s41598-021-99052-y · Cited by 12
Teramoto, H., Inui, M., & Yukawa, H. (2012) · Microbiology · doi:10.1099/mic.0.057513-0 · Cited by 12
Fenwick, M. K., & Ealick, S. E. (2016) · Biochemistry · doi:10.1021/acs.biochem.6b00626 · Cited by 12
Xu, Y., Lu, A., Guan, X., Ying, T., Pan, J., Tan, M., & Lu, J. (2024) · Food Frontiers · doi:10.1002/fft2.511 · Cited by 11
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Chow, C., Hegde, S. S., & Blanchard, J. S. (2017) · Biochemistry · doi:10.1021/acs.biochem.7b00307 · Cited by 10
Lactate dehydrogenase is the Achilles’ heel of Lyme disease bacterium Borreliella burgdorferi
Sze, C. W., Lynch, M. J., Zhang, K., Neau, D. B., Ealick, S. E., Crane, B. R., & Li, C. (2025) · mBio · doi:10.1128/mbio.03728-24 · Cited by 10
Stekhanova, T. N., Bezsudnova, E. Y., Mardanov, A. V., Osipov, E. M., Ravin, N. V., Георгиевич, С. К., & Popov, V. O. (2014) · Biochemistry (Moscow) · doi:10.1134/s0006297914010088 · Cited by 10
Sultana, K. N., & Srivastava, S. K. (2022) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2022.01.138 · Cited by 10
Sharma, R. S., Hartman, T. E., Beites, T., Kim, J.-H., Eoh, H., Engelhart, C. A., Zhu, L., Wilson, D. J., Aldrich, C. C., Ehrt, S., et al. (2023) · mBio · doi:10.1128/mbio.00340-23 · Cited by 11
Michels, P. A. M., & Avilán, L. (2011) · Molecular Microbiology · doi:10.1111/j.1365-2958.2011.07810.x · Cited by 10
Hachisuka, S.-I., Sato, T., & Atomi, H. (2018) · Journal of Bacteriology · doi:10.1128/jb.00785-17 · Cited by 10
Taniguchi, H., Imura, M., Okano, K., & Honda, K. (2019) · Microbial Cell Factories · doi:10.1186/s12934-019-1125-x · Cited by 10
Escalante-Beltrán, A., Sandoval, P. H. M., González-Astorga, C. B., Montoya-Martínez, A. C., Cubedo-Ruiz, E. A., Santoyo, G., Parra-Cota, F. I., & Santos‐Villalobos, S. D. L. (2025) · Plants · doi:10.3390/plants14132081 · Cited by 9
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Xu, G., Ma, J., Fang, Q., Peng, Q., Jiao, X., Hu, W., Zhao, Q., Kong, Y., Liu, F., Shi, X., et al. (2024) · Communications Biology · doi:10.1038/s42003-024-05921-3 · Cited by 8
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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
Effects of NAD+ in Caenorhabditis elegans Models of Neuronal Damage
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Esakova, O. A., Silakov, A., Grove, T. L., Warui, D. M., Yennawar, N. H., & Booker, S. J. (2019) · Journal of the American Chemical Society · doi:10.1021/jacs.9b02513 · Cited by 8
Losada, A. A., Méndez, C., Salas, J. A., & Olano, C. (2017) · Microbial Cell Factories · doi:10.1186/s12934-017-0709-6 · Cited by 8
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Wong, Y.-C., Naeem, R., Ghany, M. A. E., Hoh, C.-C., Pain, A., & Nathan, S. (2022) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2022.1062682 · Cited by 7
Huang, W., Xu, J.-Z., & Zhang, W. (2023) · Systems Microbiology and Biomanufacturing · doi:10.1007/s43393-023-00172-5 · Cited by 7
Afzal, M., Shafeeq, S., & Kuipers, O. P. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.01300 · Cited by 7
Liang, Z., Sun, H., Li, Y., Hu, A., Tang, Q., & Yu, H. (2023) · Environmental Microbiology · doi:10.1111/1462-2920.16484 · Cited by 7
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Crook, M., McReynolds, M. R., Wang, W., & Hanna‐Rose, W. (2014) · Developmental Dynamics · doi:10.1002/dvdy.24139 · Cited by 7
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Lebovitz, Y., & Theus, M. H. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.01162 · Cited by 7
Choueiry, F., Gold, A., Xu, R., Zhang, S., & Zhu, J. (2023) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.3c00304 · Cited by 6
Cortés, M. P., Acuña, V., Travisany, D., Siegel, A., Maass, A., & Latorre, M. (2020) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2019.00155 · Cited by 6
Mandal, H., Vijayakumar, S., Yadav, S., Singh, S. K., & Das, P. K. (2018) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2018.1552199 · Cited by 6
Minard, K. I., & McAlister-Henn, L. (2010) · Biochemistry · doi:10.1021/bi100825z · Cited by 6
Potential of exudate metabolites to predict microbial populations in beef
Hong, H., Kim, H.-J., Kim, H., Ismail, A., Choi, M., & Jo, C. (2025) · Food Research International · doi:10.1016/j.foodres.2025.116814 · Cited by 5
Chen, L., Yin, Z., Shang, L., Yuan, H., Gao, W., Wang, S., Wang, S., Hou, X., Yang, S., & Chu, H. (2025) · Clinical and Translational Medicine · doi:10.1002/ctm2.70447 · Cited by 5
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Donu, D., Sharma, C., & Cen, Y. (2022) · Biomolecules · doi:10.3390/biom12081109 · Cited by 5
c-di-GMP regulates bacterial NAD biosynthesis via targeting the transcriptional repressor NadR
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Yang, L., Wei, W., Sun, X., Li, X., Wen, X., Mao, B., Hao, R., Qiu, W., & Li, H. (2026) · Bioresource Technology · doi:10.1016/j.biortech.2026.134138 · Cited by 4
Baquero, F., del Campo, R., & Martínez, J. L. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.861603 · Cited by 4
Matsumoto, S., Biniecka, P., Bellotti, A., Duchosal, M. A., & Nahimana, A. (2023) · Cancers · doi:10.3390/cancers15030787 · Cited by 4
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Abdurasulova, I. N., & Dmitriev, A. V. (2023) · Успехи физиологических наук · doi:10.31857/s0301179823010034 · Cited by 4
Janowicz, D. M., Zwickl, B., Fortney, K. R., Katz, B. P., & Bauer, M. E. (2014) · BMC Microbiology · doi:10.1186/1471-2180-14-166 · Cited by 4
Ali, T. H., & El-Ghonemy, D. H. (2016) · 3 Biotech · doi:10.1007/s13205-015-0349-7 · Cited by 4
The function of KptA/Tpt1 gene – a minor review
Yang, S., Qu, G., Fu, B., Yang, F., Zeng, W., Cai, Y., Tao, Y., Yang, Y., Deng, X., Xiang, W., et al. (2020) · Functional Plant Biology · doi:10.1071/fp19159 · Cited by 5
Bogan, K. L., & Brenner, C. (2013) · Encyclopedia of Biological Chemistry · doi:10.1016/b978-0-12-378630-2.00103-1 · Cited by 4
Self-citationMETABOLIC PATHWAYS | Metabolism of Minerals and Vitamins
Shin, M., Umezawa, C. Y., & Shin, T. (2014) · Encyclopedia of Food Microbiology · doi:10.1016/b978-0-12-384730-0.00201-9 · Cited by 4
Abdurasulova, I. N., Chernyavskaya, E. A., Ivanov, A. B., Nikitina, V., Lioudyno, V. I., Nartova, A. A., Matsulevich, A. V., Skripchenko, E. Y., Бисага, Г. Н., Игоревич, У. В., et al. (2024) · Journal of Evolutionary Biochemistry and Physiology · doi:10.1134/s0022093024010095 · Cited by 3
Pandit, N. K., Sharma, P., Sharma, P., Rout, P. R., Mohanty, A., & Meena, S. S. (2025) · Reviews in Environmental Science and Bio/Technology · doi:10.1007/s11157-025-09753-3 · Cited by 4
Bifunctional NadC Homologue PyrZ Catalyzes Nicotinic Acid Formation in Pyridomycin Biosynthesis
Zhou, Z., Xu, Y., Huang, T., Zheng, J., Deng, Z., Dai, S., & Lin, S. (2022) · ACS Chemical Biology · doi:10.1021/acschembio.2c00773 · Cited by 3
Singh, H. B., Kaur, L., Singh, G., Singh, G., Kaur, S., Buttar, H. S., & Singh, B. (2024) · Advances in biochemistry in health and disease · doi:10.1007/978-3-031-55474-2_7 · Cited by 3
Bao, T., Weng, P., Wang, J., Cui, S., Tao, Y., Huang, J., Yang, X., & Ke, C. (2024) · Food Bioscience · doi:10.1016/j.fbio.2024.105725 · Cited by 3
Rice, J., Lautrup, S., & Fang, E. F. (2024) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-031-66768-8_4 · Cited by 4
Chowdhury, M., Ogunleye, S. C., Riman, M. M., Frank, M. W., & Abdelhamed, H. (2025) · Microbial Pathogenesis · doi:10.1016/j.micpath.2025.108001 · Cited by 2
Clinical evidence for the use of NAD+ precursors to slow aging
Khatri, S., Abdellatif, M., & Sedej, S. (2025) · Geromedicine · doi:10.70401/geromedicine.2025.0008 · Cited by 3
Wu, X., Williams, J. G., Liang, H., Gruzdev, A., Hartsell, J., Shpargel, J., Mainali, R., Fang, Y., Ji, M., Duval, C., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-68998-w · Cited by 3
In vitro characterization of the NAD+ synthetase NadE1 from Herbaspirillum seropedicae
Laskoski, K., Santos, A. R. S., Bonatto, A. C., Pedrosa, F. O., de Souza, E. M., & Huergo, L. F. (2016) · Archives of Microbiology · doi:10.1007/s00203-016-1190-z · Cited by 2
Episodic evolution of a eukaryotic NADK repertoire of ancient provenance
Vickman, O., & Erives, A. J. (2019) · PLoS ONE · doi:10.1371/journal.pone.0220447 · Cited by 3
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Zwickenpflug, W., Hornung, F., Hollaus, A., Oswald, M., Chioato, Z. L., Gudermann, T. W., & Högg, C. (2024) · Journal of the Science of Food and Agriculture · doi:10.1002/jsfa.13513 · Cited by 2
Bitew, M. A., Wawegama, N. K., Newton, H. J., & Sansom, F. M. (2019) · Pathogens and Disease · doi:10.1093/femspd/ftz066 · Cited by 2
Bacterial NadQ (COG4111) is a Nudix-like, ATP-responsive regulator of NAD biosynthesis
Minazzato, G., Gasparrini, M., Heroux, A., Sernova, N. V., Rodionov, D. A., Cianci, M., Sorci, L., & Raffaelli, N. (2022) · Journal of Structural Biology · doi:10.1016/j.jsb.2022.107917 · Cited by 2
Hympánová, M., Kucera, T., Benek, O., Korábečný, J., & Marek, J. (2020) · Military Medical Science Letters · doi:10.31482/mmsl.2020.005 · Cited by 2
Walter, B. M., Morcinek-Orłowska, J., Szulc, A., Lovering, A. L., Haycocks, J. R. J., Banzhaf, M., & Glinkowska, M. K. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.12.09.417477 · Cited by 2
A Sequence Motif Enables Widespread Use of Non-Canonical Redox Cofactors in Natural EnzymesPreprint
Saleh, S., Hsu, N.-H., Luu, E., Martin, V. C., Ng, H. J. C., Black, W. B., Kim, J., Sankaran, B., Hayes, R. L., Siegel, J. B., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.08.01.668186 · Cited by 2
Abdurasulova, I. N., Chernyavskaya, E. A., Nikitina, V., Ivanov, A. B., Lioudyno, V. I., Nartova, A. A., Matsulevich, A. V., Skripchenko, E. Y., Бисага, Г. Н., Игоревич, У. В., et al. (2024) · Журнал эволюционной биохимии и физиологии · doi:10.31857/s0044452924010098 · Cited by 1
The NARly side of whole-body NAD homeostasis
Brenner, C. (2025) · Cell Metabolism · doi:10.1016/j.cmet.2025.06.003 · Cited by 1
Self-citationKing, C. G., Cheng, K.-J., & Breaker, R. R. (2025) · RNA · doi:10.1261/rna.080744.125 · Cited by 1
Yang, Y., Yang, R., Chen, Y., He, C., Zhang, Y., Jing, H., Zhang, J., Wang, H., Liang, J., Deng, Z., et al. (2026) · Gut · doi:10.1136/gutjnl-2025-336161 · Cited by 2
The NAD salvage pathway enzyme NMNAT-C sustains dark-phase NAD+ homeostasis in cyanobacteria
Zhang, F., Zhang, H., Wang, P., Qi, Y., Li, H., Zhu, L., Huang, G., Xia, Y., & Cai, Z. (2026) · PLANT PHYSIOLOGY · doi:10.1093/plphys/kiag143 · Cited by 1
Tracing NAD+ metabolism uncovers adaptive coordination between host and microbiome during colitis
Alsaadi, A. I., Wehkamp, L., Pothakamury, A. A., Yahia, M. S., Prasad, P., Gilloteau, C., Sadler, J., Smith, J. D., Jenkins, B. C., Diven, G. S., et al. (2026) · Cell Reports · doi:10.1016/j.celrep.2026.117730 · Cited by 1
Screening of Natural High-producing NMN strains and Microbial Synthesis of NMN by Nampt
Li, C., Long, Z., Zhang, H., Lin, Y., & Zhao, L. (2023) · Food Nutrition Chemistry · doi:10.18686/fnc.v1i1.7 · Cited by 1
Ávila-Jiménez, S., Contreras-Rodríguez, L. E., Granados‐Ramírez, C. G., Monroy, Z. J. R., & Ramírez-Hernández, M. H. (2021) · Revista Colombiana de Química · doi:10.15446/rev.colomb.quim.v50n1.89863 · Cited by 1
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
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