The DOI matches its Crossref record; 46 of the 46 references it cites were found in a registry or an index.
Elevation of Cellular NAD Levels by Nicotinic Acid and Involvement of Nicotinic Acid Phosphoribosyltransferase in Human Cells
Open accessAbstract
NAD plays critical roles in various biological processes through the function of SIRT1. Although classical studies in mammals showed that nicotinic acid (NA) is a better precursor than nicotinamide (Nam) in elevating tissue NAD levels, molecular details of NAD synthesis from NA remain largely unknown. We here identified NA phosphoribosyltransferase (NAPRT) in humans and provided direct evidence of tight link between NAPRT and the increase in cellular NAD levels. The enzyme was abundantly expressed in the small intestine, liver, and kidney in mice and mediated [(14)C]NAD synthesis from [(14)C]NA in human cells. In cells expressing endogenous NAPRT, the addition of NA but not Nam almost doubled cellular NAD contents and decreased cytotoxicity by H(2)O(2). Both effects were reversed by knockdown of NAPRT expression. These results indicate that NAPRT is essential for NA to increase cellular NAD levels and, thus, to prevent oxidative stress of the cells. Kinetic analyses revealed that NAPRT, but not Nam phosphoribosyltransferase (NamPRT, also known as pre-B-cell colony-enhancing factor or visfatin), is insensitive to the physiological concentration of NAD. Together, we conclude that NA elevates cellular NAD levels through NAPRT function and, thus, protects the cells against stress, partly due to lack of feedback inhibition of NAPRT but not NamPRT by NAD. The ability of NA to increase cellular NAD contents may account for some of the clinically observed effects of the vitamin and further implies a novel application of the vitamin to treat diseases such as those associated with the depletion of cellular NAD pools.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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?
In the citing paper
“Experimental evidence suggests that blood NA and NAM are able to cross the plasma membrane, while blood NAD+ cannot be taken up by cells directly but needs to be converted to smaller uncharged molecules to enter the cells (Hara et al., 2007; Ratajczak et al., 2016).”
From NAD+ in Brain Aging and Neurodegenerative Disorders (2019) · cites this paper as Hara et al., 2007
In the citing paper
“trigonelline or NA failed to raise NAD+ levels in HepG2 (ref. 34) and C2C12 cells, which have low NAPRT expression (Extended Data Fig. 1g,h)”
From Trigonelline Is an NAD+ Precursor That Improves Muscle Function during Ageing and Is Reduced in Human Sarcopenia (2024) · cites this paper as [34]
Citations
Cites
1 retracted
Visfatin: A Protein Secreted by Visceral Fat That Mimics the Effects of Insulin
Fukuhara, A., Matsuda, M., Nishizawa, M., Segawa, K., Tanaka, M., Kishimoto, K., Matsuki, Y., Murakami, M., Ichisaka, T., Murakami, H., et al. (2005) · Science · doi:10.1126/science.1097243 · Cited by 1,906
RetractedSmall molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan
Howitz, K. T., Bitterman, K. J., Cohen, H. Y., Lamming, D. W., Lavu, S., Wood, J. G., Zipkin, R. E., Chung, P., Kisielewski, A., Zhang, L.-L., et al. (2003) · Nature · doi:10.1038/nature01960 · Cited by 3,796
Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase
Brunet, A., Sweeney, L. B., Sturgill, J. F., Chua, K. F., Greer, P. L., Lin, Y., Tran, H., Ross, S. E., Mostoslavsky, R., Cohen, H. Y., et al. (2004) · Science · doi:10.1126/science.1094637 · Cited by 3,239
Nutrient control of glucose homeostasis through a complex of PGC-1α and SIRT1
Rodgers, J. T., Lerin, C., Haas, W., Gygi, S. P., Spiegelman, B. M., & Puigserver, P. (2005) · Nature · doi:10.1038/nature03354 · Cited by 3,160
Modulation of NF‐κB‐dependent transcription and cell survival by the SIRT1 deacetylase
Yeung, F., Hoberg, J. E., Ramsey, C. S., Keller, M. D., Jones, D. R., Frye, R. A., & Mayo, M. W. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600244 · Cited by 2,750
hSIR2SIRT1 Functions as an NAD-Dependent p53 Deacetylase
Vaziri, H., Dessain, S. K., Eaton, E. N., Imai, S., Frye, R. A., Pandita, T. K., Guarente, L., & Weinberg, R. A. (2001) · Cell · doi:10.1016/s0092-8674(01)00527-x · Cited by 2,690
Negative Control of p53 by Sir2α Promotes Cell Survival under Stress
Luo, J., Nikolaev, A. Y., Imai, S.-I., Chen, D., Su, F., Shiloh, A., Guarente, L., & Gu, W. (2001) · Cell · doi:10.1016/s0092-8674(01)00524-4 · Cited by 2,081
Sirt1 promotes fat mobilization in white adipocytes by repressing PPAR-γ
Picard, F., Kurtev, M. V., Chung, N., Topark‐Ngarm, A., Senawong, T., de Oliveira, R. M., Leid, M. E., McBurney, M. W., & Guarente, L. (2004) · Nature · doi:10.1038/nature02583 · Cited by 1,943
The Therapeutic Potential of Poly(ADP-Ribose) Polymerase Inhibitors
Virág, L., & Szabó, C. (2002) · Pharmacological Reviews · doi:10.1124/pr.54.3.375 · Cited by 1,373
Mammalian SIRT1 Represses Forkhead Transcription Factors
Motta, M. C., Divecha, N., Lemieux, M. E., Kamel, C., Chen, D., Gu, W. J., Bultsma, Y., McBurney, M. W., & Guarente, L. (2004) · Cell · doi:10.1016/s0092-8674(04)00126-6 · Cited by 1,366
Research works printed but not linked: 9
- Hasmann, 2003, Cancer Res., 63, 7436
- Magni, 1999, Adv. Enzymol. Relat. Areas Mol. Biol., 73, 135
- Samal, 1994, Mol. Cell. Biol., 14, 1431
- Jackson, 1995, J. Nutr., 125, 1455
- Shibata, 1986, Agric. Biol. Chem., 50, 3037
- Ishiyama, 1995, In Vitro Toxicol., 8, 187
- Hayakawa, 1984, Agric. Biol. Chem., 48, 445
- Hayakawa, 1984, Agric. Biol. Chem., 48, 455
- Trueblood, 2000, Am. J. Physiol., 279, H764
Cited by
Sorted by citations
Items 101–200 of 206
Hughes-Large, J. M., Pang, D., Robson, D. L., Chan, P., Toma, J., & Borradaile, N. M. (2014) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2014.10.090 · Cited by 35
AMPK phosphorylates NAMPT to regulate NAD + homeostasis under ionizing radiation
Liao, X., Huang, X., Li, X., Qiu, X., Li, M., Liu, R. R., He, T., & Tang, Q. (2022) · Open Biology · doi:10.1098/rsob.220213 · Cited by 37
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 34
Diabetes Mellitus: Channeling Care through Cellular Discovery
Maiese, K., Shang, Y., Chong, Z. Z., & Hou, J. (2010) · Current Neurovascular Research · doi:10.2174/156720210790820217 · Cited by 32
Quinoline Quest: Kynurenic Acid Strategies for Next-Generation Therapeutics via Rational Drug Design
Tanaka, M., Szatmári, I., & Vécsei, L. (2025) · Pharmaceuticals · doi:10.3390/ph18050607 · Cited by 37
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
PARP and other prospective targets for poisoning cancer cell metabolism
Michels, J., Obrist, F., Castedo, M., Vitale, I., & Kroemer, G. (2014) · Biochemical Pharmacology · doi:10.1016/j.bcp.2014.08.026 · Cited by 28
Duarte-Pereira, S., Silva, S. S., Azevedo, L., Castro, L., Amorim, A., & Silva, R. M. (2014) · Scientific Reports · doi:10.1038/srep06311 · Cited by 29
Channeling Nicotinamide Phosphoribosyltransferase (NAMPT) to Address Life and Death
Reddy, V. G., Krider, I. S., Alves, E. T. M., Courey, J. M., Laham, M. S., & Thatcher, G. R. J. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c02112 · Cited by 27
Regulation of Cancer and Cancer-Related Genes via NAD +
Sharif, T., Martell, E., Dai, C., Ghassemi-Rad, M. S., Kennedy, B. E., Lee, P. W. K., & Gujar, S. A. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7478 · Cited by 25
NAD metabolism and heart failure: Mechanisms and therapeutic potentials
Walker, M. A., & Tian, R. (2024) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2024.07.008 · Cited by 25
NADH elevation during chronic hypoxia leads to VHL-mediated HIF-1α degradation via SIRT1 inhibition
Joo, H.-Y., Jung, J. K., Kim, M., Woo, S. R., Jeong, J. M., Park, E., Kim, Y., Park, J., Kim, J., Yun, M., et al. (2023) · Cell & Bioscience · doi:10.1186/s13578-023-01130-3 · Cited by 25
Amici, A., Grolla, A. A., Grosso, E. D., Bellini, R., Bianchi, M., Travelli, C., Garavaglia, S., Sorci, L., Raffaelli, N., Ruggieri, S., et al. (2017) · Cell chemical biology · doi:10.1016/j.chembiol.2017.03.010 · Cited by 24
Zhang, X., Zhang, Y., Sun, A., & Ge, J. (2021) · Genes & Diseases · doi:10.1016/j.gendis.2021.04.001 · Cited by 24
Din, M., Barozai, M. Y. K., & Baloch, I. A. (2016) · Gene Reports · doi:10.1016/j.genrep.2016.08.010 · Cited by 23
Hwang, D., Jo, H., Ma, S.-H., & Lim, Y. (2018) · Food and Chemical Toxicology · doi:10.1016/j.fct.2018.06.039 · Cited by 23
Suzuki, E., Okuda, H., Nishida, K., Fujimoto, S., & Nagasawa, K. (2010) · Life Sciences · doi:10.1016/j.lfs.2010.02.019 · Cited by 23
Bruckbauer, A., Banerjee, J., Cao, Q., Cui, X., Jing, J., Zha, L., Li, F., Xue, B., Shi, H., & Zemel, M. B. (2017) · Europe PMC (PubMed Central) · Cited by 22
NAD+ Precursors and Antioxidants for the Treatment of Amyotrophic Lateral Sclerosis
Obrador, E., Palmer, R. S., López‐Blanch, R., Dellinger, R. W., & Estrela, J. M. (2021) · Biomedicines · doi:10.3390/biomedicines9081000 · Cited by 23
Identification of NAPRT Inhibitors with Anti-Cancer Properties by In Silico Drug Discovery
Ghanem, M. S., Caffa, I., Río, A. D., Franco, J., Parenti, M. D., Monacelli, F., Cea, M., Khalifa, A., Nahimana, A., Duchosal, M. A., et al. (2022) · Pharmaceuticals · doi:10.3390/ph15070848 · Cited by 23
Urbański, A., Johnston, P. R., Bittermann, E., Keshavarz, M., Paris, V., Walkowiak‐Nowicka, K., Konopińska, N., Marciniak, P., & Rolff, J. (2022) · Scientific Reports · doi:10.1038/s41598-022-21605-6 · Cited by 21
Feng, S., Guo, L., Wang, H., Yang, S., & Liu, H. (2023) · Communications Biology · doi:10.1038/s42003-023-04613-8 · Cited by 20
NAD+-targeting by bacteria: an emerging weapon in pathogenesis
Roussin, M., & Salcedo, S. P. (2021) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuab037 · Cited by 19
The Significance of NAD+ Biosynthesis Alterations in Acute Kidney Injury
Clark, A. J., Saadé, M. C., & Parikh, S. M. (2022) · Seminars in Nephrology · doi:10.1016/j.semnephrol.2022.10.013 · Cited by 18
Hara, N., Osago, H., Hiyoshi, M., Kobayashi‐Miura, M., & Tsuchiya, M. (2019) · PLoS ONE · doi:10.1371/journal.pone.0214000 · Cited by 21
Self-citationNicotinamide as a Foundation for Treating Neurodegenerative Disease and Metabolic Disorders
Maiese, K. (2021) · Current Neurovascular Research · doi:10.2174/1567202617999210104220334 · Cited by 23
Nicotinamide breaks effector CD8 T cell responses by targeting mTOR signaling
Agliano, F., Karginov, T. A., Ménoret, A., Provatas, A. A., & Vella, A. T. (2022) · iScience · doi:10.1016/j.isci.2022.103932 · Cited by 18
Dosing profile profoundly influences nicotinic acid's ability to improve metabolic control in rats
Kroon, T., Kjellstedt, A., Thalén, P., Gabrielsson, J., & Oakes, N. D. (2015) · Journal of Lipid Research · doi:10.1194/jlr.m058149 · Cited by 18
Niacin prevents mitochondrial oxidative stress caused by sub-chronic exposure to methylmercury
Pereira, L. C., de Paula, E. S., Pazin, M., Carneiro, M. F. H., Grotto, D., Barbosa, F., & Dorta, D. J. (2018) · Drug and Chemical Toxicology · doi:10.1080/01480545.2018.1497045 · Cited by 18
The Role of GPR109a Signaling in Niacin Induced Effects on Fed and Fasted Hepatic Metabolism
Geisler, C. E., Miller, K. E., Ghimire, S., & Renquist, B. J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22084001 · Cited by 18
Nicotinamide: Oversight of Metabolic Dysfunction Through SIRT1, mTOR, and Clock Genes
Maiese, K. (2020) · Current Neurovascular Research · doi:10.2174/1567202617999201111195232 · Cited by 20
Cole, J., Guiot, M., Gravel, M., Bernier, C., Shore, G. C., & Roulston, A. (2017) · Oncotarget · doi:10.18632/oncotarget.20840 · Cited by 17
Sobriety and Satiety: Is NAD+ the Answer?
Braidy, N., Villalva, M. D., & van Eeden, S. (2020) · Antioxidants · doi:10.3390/antiox9050425 · Cited by 17
Faculty of Bioscience Engineering
Coussement, J. (2014) · Cited by 16
NAD+ Therapeutics and Skeletal Muscle Adaptation to Exercise in Humans
Campelj, D. G., & Philp, A. (2022) · Sports Medicine · doi:10.1007/s40279-022-01772-2 · Cited by 20
Jonsson, B. H. (2018) · Nutrients · doi:10.3390/nu10020134 · Cited by 15
Ciarlo, E., Joffraud, M., Hayat, F., Giner, M. P., Giroud‐Gerbetant, J., Sanchez-Garcia, J. L., Rumpler, M., Moco, S., Migaud, M. E., & Cantó, C. (2022) · Nutrients · doi:10.3390/nu14132752 · Cited by 15
The role of NAD metabolism in neuronal differentiation
Neves, D., Goodfellow, B. J., Vieira, S. I., & Silva, R. M. (2022) · Neurochemistry International · doi:10.1016/j.neuint.2022.105402 · Cited by 15
Nicotinamide adenine dinucleotide and the sirtuins caution: Pro‐cancer functions
Palmer, R. D., & Vaccarezza, M. (2021) · Aging Medicine · doi:10.1002/agm2.12184 · Cited by 14
Yang, N.-C., Cho, Y.-H., & Lee, I. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms21010142 · Cited by 16
Structure-Based Identification and Biological Characterization of New NAPRT Inhibitors
Franco, J., Piacente, F., Walter, M., Fratta, S., Ghanem, M. S., Benzi, A., Caffa, I., Kurkin, A. V., Altieri, A., Herr, P., et al. (2022) · Pharmaceuticals · doi:10.3390/ph15070855 · Cited by 14
Centrosome Loss Triggers a Transcriptional Program To Counter Apoptosis-Induced Oxidative Stress
Poulton, J. S., McKay, D. J., & Peifer, M. A. (2019) · Genetics · doi:10.1534/genetics.119.302051 · Cited by 14
Reducing Oxidative Stress and Enhancing Neurovascular Longevity During Diabetes Mellitus
Maiese, K., Chong, Z. Z., & Li, F. (2009) · Oxford University Press eBooks · doi:10.1093/acprof:oso/9780195326697.003.0022 · Cited by 14
Shen, W., Wan, X., Hou, J., Liu, Z., Mao, G., Xu, X., Yu, C., Zhu, X., & Ju, Z. (2022) · Life Medicine · doi:10.1093/lifemedi/lnac031 · Cited by 14
Could Exercise Metabolomics Pave the Way for Gymnomimetics?
Burke, M. F., Dunbar, R. L., & Rader, D. J. (2010) · Science Translational Medicine · doi:10.1126/scitranslmed.3001188 · Cited by 13
Jiang, C., Zhou, Y., Yan, L., Zheng, J., Wang, X., Li, J., & Jiang, X. (2023) · Frontiers in Oncology · doi:10.3389/fonc.2023.1051641 · Cited by 12
Importance of NAD+ Anabolism in Metabolic, Cardiovascular and Neurodegenerative Disorders
Helman, T. J., & Braidy, N. (2022) · Drugs & Aging · doi:10.1007/s40266-022-00989-0 · Cited by 13
Ni, J., Zhang, J., Liu, J., Fan, L., Xiao, L., Yu, H., & Sun, G. (2022) · Hematological Oncology · doi:10.1002/hon.3093 · Cited by 11
Miljkovic, M., Seguin, A., Jia, X., Cox, J. E., Catrow, J. L., Bergonia, H. A., Phillips, J. D., Stephens, W. Z., & Ward, D. M. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.104877 · Cited by 11
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 12
Afanador, G. A., Muench, S. P., McPhillie, M. J., Fomovska, A., Schön, A., Zhou, Y., Cheng, G., Stec, J., Freundlich, J. S., Shieh, H.-M., et al. (2013) · Biochemistry · doi:10.1021/bi400945y · Cited by 11
Wang, Y., Li, Q., Ma, Z., Xu, H., Peng, F., Chen, B., Ma, B., Qin, L., Lan, J., Li, Y., et al. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242115666 · Cited by 10
Bennetzen, M. V., Košař, M., Bunkenborg, J., Payne, M., Bártková, J., Lindström, M. S., Lukas, J., Andersen, J., Bártek, J., & Larsen, D. H. (2018) · Cell Cycle · doi:10.1080/15384101.2018.1515552 · Cited by 10
Noronha, K. J., Lucas, K. N., Paradkar, S., Edmonds, J., Friedman, S., Murray, M. A., Liu, S., Sajed, D. P., Sachs, C. R., Spurrier, J. M., et al. (2024) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-23-1003 · Cited by 9
Sauer, H., Kampmann, H., Khosravi, F., Sharifpanah, F., & Wartenberg, M. (2020) · Clinical and Experimental Pharmacology and Physiology · doi:10.1111/1440-1681.13452 · Cited by 8
Colombo, G., Gelardi, E. L. M., Balestrero, F. C., Moro, M., Travelli, C., & Genazzani, A. A. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.758320 · Cited by 9
Petrović, K., Djoković, R., Cincović, M., Hristovska, T., Lalović, M., Petrovic, M. Ž., Majkić, M., Marinković, M. D., Anđušić, L., Devečerski, G., et al. (2022) · Animals · doi:10.3390/ani12121524 · Cited by 9
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
González, M. C., Romero, J. M., Ingaramo, M., Sosa, C. J. M., Curtino, J. A., & Carrizo, M. E. (2016) · FEBS Letters · doi:10.1002/1873-3468.12242 · Cited by 8
Hara, N., Shibata, T., Osago, H., Yamada, K., & Tsuchiya, M. (2014) · Journal of Nutritional Science and Vitaminology · doi:10.3177/jnsv.60.17 · Cited by 8
Self-citationNAD+ metabolism restriction boosts high-dose melphalan efficacy in patients with multiple myeloma
Soncini, D., Becherini, P., Ladisa, F., Ravera, S., Chedere, A., Gelli, E., Giorgetti, G., Martinuzzi, C., Piacente, F., Mastracci, L., et al. (2024) · Blood Advances · doi:10.1182/bloodadvances.2024013425 · Cited by 7
Maiese, K. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-822467-0.00006-1 · Cited by 9
Fan, Y., Xue, M., Shan, T., Bai, Y., Zhang, H., Liu, M., Wang, P., Liang, X., & Liang, H. (2023) · Food Bioscience · doi:10.1016/j.fbio.2023.103454 · Cited by 6
Distinct Capabilities in NAD Metabolism Mediate Resistance to NAMPT Inhibition in Glioblastoma
Perryman, R., Chau, T. W., DeFelice, J., O’Neill, K., & Syed, N. (2024) · Cancers · doi:10.3390/cancers16112054 · Cited by 6
Wang, N., Pan, D., Wang, X., Su, M., Wang, X., Yan, Q., Sun, G., & Wang, S. (2022) · Nutrients · doi:10.3390/nu14224916 · Cited by 5
Minazzato, G., Marangoni, E., Fortunato, C., Petrelli, R., Cappellacci, L., Bello, F. D., Sorci, L., Gasparrini, M., Piacente, F., Bruzzone, S., et al. (2023) · Molecules · doi:10.3390/molecules28030961 · Cited by 5
Zhu, L., Liu, H., Dou, Y., Luo, Q., Gu, L., Liu, X., Zhou, Q., Han, J., & Wang, F. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24097756 · Cited by 5
Probing the Druggability Limits for Enzymes of the NAD Biosynthetic Network in Glioma
Padiadpu, J., Mishra, M., Sharma, E., Mala, U., Somasundaram, K., & Chandra, N. R. (2016) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.5b00733 · Cited by 5
Baldassarri, C., Giorgioni, G., Piergentili, A., Quaglia, W., Fontana, S., Mammoli, V., Minazzato, G., Marangoni, E., Gasparrini, M., Sorci, L., et al. (2023) · Pharmaceuticals · doi:10.3390/ph16020189 · Cited by 4
Deane, C. S., Willis, C. R. G., Gallagher, I. J., Brook, M. S., Gharahdaghi, N., Wylie, L. J., Wilkinson, D. J., Smith, K. E., Atherton, P. J., & Etheridge, T. (2024) · Translational Exercise Biomedicine · doi:10.1515/teb-2024-0030 · Cited by 4
Isolation and Characterization of the Anticancer Gene Organic Cation Transporter Like-3 (ORCTL3)
AbuAli, G., & Grimm, S. (2014) · Advances in experimental medicine and biology · doi:10.1007/978-1-4471-6458-6_11 · Cited by 4
Yang, Y., Liu, Z., Zhao, B., Joseph, S., Ma, Y., Xu, H., & Cheng, H. (2021) · Natural Product Communications · doi:10.1177/1934578x211045465 · Cited by 4
Oyama, T., Yamamoto, T., Kameda, T., Kamiya, T., Abe, H., Abe, T., & Tanuma, S. (2024) · Life · doi:10.3390/life14030413 · Cited by 4
Metabolic Alterations in NADSYN1-Deficient Cells
Meijer, N. W. F., Gerrits, J., Zwakenberg, S., Zwartkruis, F. J. T., Verhoeven‐Duif, N. M., & Jans, J. J. M. (2023) · Metabolites · doi:10.3390/metabo13121196 · Cited by 3
Gaertner, K., Tapanainen, R., Saari, S., Fekete, Z., Goffart, S., Pohjoismäki, J., & Dufour, É. (2025) · Experimental Cell Research · doi:10.1016/j.yexcr.2025.114466 · Cited by 3
Pharmacological Nicotinamide: Mechanisms Centered Around SIRT1 Activity
Hwang, E. S. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-813939-4.00029-2 · Cited by 3
Rani, K. G. A., Soares, N. C., Rahman, B., Giddey, A. D., Al-Hroub, H. M., Semreen, M. H., & Kawas, S. A. (2025) · Clinical Proteomics · doi:10.1186/s12014-024-09520-6 · Cited by 2
Wang, M., Zhao, X., Wang, H., Liu, J., Ren, J., Gao, M., Cheng, F.-E., Chen, P., Yao, W., Cao, Y., et al. (2026) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2026.150704 · Cited by 2
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
Nora, E.-S., Eman, M. E., Hanaa, A.-F., & El‐Ansary, M. (2015) · Journal of Scientific Research in Science /Journal of Scientific Research in Science · doi:10.21608/jsrs.2015.24858 · Cited by 2
Palikhe, S., & Nakagawa, T. (2022) · Springer eBooks · doi:10.1007/978-981-16-7977-3_8 · Cited by 1
Hwang, E. S. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-18722-3.00011-6 · Cited by 1
Kocemba‐Pilarczyk, K. A., Ostrowska, B., Trojan, S., & Dudzik, P. (2025) · Pharmacological Reports · doi:10.1007/s43440-025-00768-9 · Cited by 2
Niacin and microvascular endothelial cell response to fatty acid excess and hypoxia
Pang, D. (2014) · Scholarship@Western (Western University) · Cited by 1
Shackelford, R. E., Abdelbaqi, M. Q., Anga, A., & Cotelignam, J. (2008) · Bioscience hypotheses · doi:10.1016/j.bihy.2008.06.013
Haverty, P. M., Liederer, B. M., Liang, X., Yauch, R. L., O’Brien, T., Bourgon, R., Koeppen, H., & Belmont, L. D. (2013)
Ruiz‐Rodado, V. (2016) · DMU Open Research Archive (De Montfort University)
Katsyuba, E., & Auwerx, J. H. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-813499-3.00003-4
Hristovska, T., Cincović, M. R., Dodovski, P., Karabolovski, N., Dameski, P., Pejcinovska, N., Zdraveski, I., Ristevski, M., Angelovska, M., & Jankulovska-Petkovska, M. (2023) · Horizons - International Scientific Journal · doi:10.20544/horizons.1.1.23.p01
Metabolism and Receptor Mechanisms of Niacin Action
Boronovskiy, S. E., Сергеевна, К. В., & Nartsissov, Y. R. (2023) · Tsitologiya · doi:10.31857/s0041377123060032
Gopalakrishnan, A. R. K., Soares, N. C., Rahman, B., Giddey, A. D., Al-Hroub, H. M., Semreen, M. H., & Kawas, S. A. (2024) · Research Square · doi:10.21203/rs.3.rs-4301082/v1
Joo, H.-Y., Jung, J. K., Kim, M.-Y., Woo, S. R., Jeong, J. M., Park, E.-R., Kim, Y.-M., Park, J., Kim, J., Yun, M., et al. (2023) · Figshare · doi:10.6084/m9.figshare.24225237
Joo, H.-Y., Jung, J. K., Kim, M.-Y., Woo, S. R., Jeong, J. M., Park, E.-R., Kim, Y.-M., Park, J., Kim, J., Yun, M., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26621263
Joo, H.-Y., Jung, J. K., Kim, M.-Y., Woo, S. R., Jeong, J. M., Park, E.-R., Kim, Y.-M., Park, J., Kim, J., Yun, M., et al. (2024) · Figshare · doi:10.6084/m9.figshare.24225253
Mohan, N. V., Muthusamy, S., & Jothi, A. (2025) · Journal of Computational Biophysics and Chemistry · doi:10.1142/s2737416526500043
Metadata
- Authors
- Hara, N., Yamada, K., Shibata, T., Osago, H., Hashimoto, T., & Tsuchiya, M.
- Affiliations
- Shimane University (JP)
- Corresponding author
- Hara, Nobumasa
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2007-08
- Volume
- 282
- Issue
- 34
- Pages
- 24574-24582
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2083287520
- Cited by
- 205
- References
- 46
- Citations by year
- 2026: 3 · 2025: 7 · 2024: 15 · 2023: 14 · 2022: 23 · 2021: 15 · 2020: 11 · 2019: 7 · 2018: 16 · 2017: 10 · 2016: 8 · 2015: 10 · 2014: 11 · 2013: 8 · 2012: 4
- FWCI
- 4.80
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- 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 › Nursing › Nutrition and Dietetics › Folate and B Vitamins Research
- Keywords
- nicotinic acid, NAD levels, visfatin, NAD biosynthesis, SIRT1, oxidative stress, hydrogen peroxide cytotoxicity, nicotinamide
- MeSH terms
- Animals, HeLa Cells, Humans, Kinetics, Mice, Inbred BALB C, Models, Biological, Molecular Sequence Data, NAD, Niacin, Pentosyltransferases, Tissue Distribution, Oxidative Stress, RNA, Small Interfering, Mice, Rats
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