The DOI matches its Crossref record; 61 of the 61 references it cites were found in a registry or an index.
The NAD Biosynthesis Pathway Mediated by Nicotinamide Phosphoribosyltransferase Regulates Sir2 Activity in Mammalian Cells
Open accessAbstract
Recent studies have revealed new roles for NAD and its derivatives in transcriptional regulation. The evolutionarily conserved Sir2 protein family requires NAD for its deacetylase activity and regulates a variety of biological processes, such as stress response, differentiation, metabolism, and aging. Despite its absolute requirement for NAD, the regulation of Sir2 function by NAD biosynthesis pathways is poorly understood in mammals. In this study, we determined the kinetics of the NAD biosynthesis mediated by nicotinamide phosphoribosyltransferase (Nampt) and nicotinamide/nicotinic acid mononucleotide adenylyltransferase (Nmnat), and we examined its effects on the transcriptional regulatory function of the mouse Sir2 ortholog, Sir2alpha, in mouse fibroblasts. We found that Nampt was the rate-limiting component in this mammalian NAD biosynthesis pathway. Increased dosage of Nampt, but not Nmnat, increased the total cellular NAD level and enhanced the transcriptional regulatory activity of the catalytic domain of Sir2alpha recruited onto a reporter gene in mouse fibroblasts. Gene expression profiling with oligonucleotide microarrays also demonstrated a significant correlation between the expression profiles of Nampt- and Sir2alpha-overexpressing cells. These findings suggest that NAD biosynthesis mediated by Nampt regulates the function of Sir2alpha and thereby plays an important role in controlling various biological events in mammals.
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
“NMN is an intermediate in the salvage pathway and can be converted to NAD+, bypassing a catalysis of nicotinamide phosphoribosyltransferase (NAMPT), a rate-limiting enzyme in this pathway (10).”
From Nicotinamide riboside and nicotinamide mononucleotide facilitate NAD + synthesis via enterohepatic circulation (2025) · cites this paper as [10]
The cited source says what the claim attributes to it.
In the citing paper
“NMN is a substrate for nicotinamide mononucleotide adenylyltransferase (NMNAT), which is an enzyme that converts NMN and adenosine triphosphate to NAD+ and inorganic pyrophosphate (10).”
From Nicotinamide riboside and nicotinamide mononucleotide facilitate NAD + synthesis via enterohepatic circulation (2025) · cites this paper as [10]
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
Efficient selection for high-expression transfectants with a novel eukaryotic vector
Niwa, H., Yamamura, K., & Miyazaki, J. (1991) · Gene · doi:10.1016/0378-1119(91)90434-d · Cited by 5,149
Yang, Y., Dudoit, S., Luu, P., Lin, D., Peng, V., Ngai, J., & Speed, T. (2002) · Nucleic Acids Research · doi:10.1093/nar/30.4.e15 · Cited by 3,722
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
Self-citationStress-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
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
Self-citationKaeberlein, M., McVey, M., & Guarente, L. (1999) · Genes & Development · doi:10.1101/gad.13.19.2570 · Cited by 2,253
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
Self-citationSirt1 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
Calorie restriction promotes mammalian cell survival by inducing the SIRT1 deacetylase
Cohen, H. Y., Miller, C., Bitterman, K. J., Wall, N. R., Hekking, B., Kessler, B., Howitz, K. T., Gorospe, M., de Cabo, R., & Sinclair, D. A. (2004) · Science · doi:10.1126/science.1099196 · Cited by 1,924
Research works printed but not linked: 4
- Magni, 1999, Adv. Enzymol. Relat. Areas Mol. Biol., 73, 135
- Samal, 1994, Mol. Cell. Biol., 14, 1431
- Neubert, 1964, Biochim. Biophys. Acta, 92, 610
- Picard, 2004, Nature, 429, 771, 10.1038/nature02583 · DOI
Cited by
Sorted by citations
Items 501–600 of 999
McCarty, M. F., Luján, L. M. L., & Assanga, S. B. I. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23094776 · Cited by 36
Suzuki‐Yamamoto, M., Mimura, T., & Ashihara, H. (2006) · Physiologia Plantarum · doi:10.1111/j.1399-3054.2006.00753.x · Cited by 34
Catalysis and Mechanistic Insights into Sirtuin Activation
Dittenhafer‐Reed, K. E., Feldman, J. L., & Denu, J. M. (2010) · ChemBioChem · doi:10.1002/cbic.201000434 · Cited by 36
Chen, G., Su, H., Lin, Y., Po-Yen, T., Chyuan, J., & Chao, P. (2016) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2016.03.009 · Cited by 36
Tam, I., Dzierżęga‐Lęcznar, A., & Stȩpień, K. B. (2019) · Experimental Dermatology · doi:10.1111/exd.13908 · Cited by 34
LMO2 activation by deacetylation is indispensable for hematopoiesis and T-ALL leukemogenesis.
Morishima, T., Krahl, A.-C., Nasri, M., Xu, Y., Aghaallaei, N., Findik, B., Klimiankou, M., Ritter, M., Hartmann, M., Gloeckner, C., et al. (2019) · Blood · doi:10.1182/blood.2019000095 · Cited by 24
Li, Z., Shan, L., Yu, D., & Zhang, F. (2023) · Colloids and Surfaces A Physicochemical and Engineering Aspects · doi:10.1016/j.colsurfa.2023.133024 · Cited by 33
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
Keshari, K. R., Wilson, D. M., Criekinge, M. V., Sriram, R., Koelsch, B. L., Wang, Z. J., VanBrocklin, H. F., Peehl, D. M., O'Brien, T., Sampath, D., et al. (2015) · The Prostate · doi:10.1002/pros.23036 · Cited by 33
Luo, C., Ding, W., Yang, C., Zhang, W., Liu, X., & Deng, H. (2022) · Journal of Proteome Research · doi:10.1021/acs.jproteome.2c00167 · Cited by 33
The function of nicotinamide phosphoribosyl transferase (NAMPT) and its role in diseases
Peng, A., Li, J., Xing, J., Yao, Y., Niu, X., & Zhang, K. (2024) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2024.1480617 · Cited by 39
Zerp, S. F., Vens, C., Floot, B., Verheij, M., & van Triest, B. (2014) · Radiotherapy and Oncology · doi:10.1016/j.radonc.2013.10.039 · Cited by 32
Wang, X., Zhang, Z., Zhang, N., Li, H., Zhang, L., Baines, C. P., & Ding, S. (2019) · Journal of Neurochemistry · doi:10.1111/jnc.14878 · Cited by 34
Xu, W., Li, L., & Zhang, L. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.00901 · Cited by 35
Nutritional and hormonal regulation of uncoupling protein 2
Yonezawa, T., Kurata, R., Hosomichi, K., Kono, A., Kimura, M., & Inoko, H. (2009) · IUBMB Life · doi:10.1002/iub.264 · Cited by 32
Wenzel, U. (2006) · Genes & Nutrition · doi:10.1007/bf02829950 · Cited by 35
Wang, X., Li, H., & Ding, S. (2016) · Scientific Reports · doi:10.1038/srep32416 · Cited by 32
Ahn, J., Lee, H., Jung, C. H., Choi, W. H., & Ha, T. Y. (2017) · Oncotarget · doi:10.18632/oncotarget.16974 · Cited by 31
Abdelwahed, O. M., Tork, O. M., el Din, M. G., Rashed, L. A., & Zickri, M. B. (2018) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2018.02.002 · Cited by 34
Shi, C., Wu, H., Du, D., Im, H., Zhang, Y., Hu, B., Chen, H., Wang, X., Liu, Y., Cao, P., et al. (2018) · Cellular Physiology and Biochemistry · doi:10.1159/000493843 · Cited by 31
Updated Functional Roles of NAMPT in Carcinogenesis and Therapeutic Niches
Lin, T. (2022) · Cancers · doi:10.3390/cancers14092059 · Cited by 31
Mahajan, S. S., Leko, V., Simon, J. A., & Bedalov, A. (2011) · Handbook of experimental pharmacology · doi:10.1007/978-3-642-21631-2_11 · Cited by 32
Role of adipokines (omentin and visfatin) in coronary artery disease
Ali, S., Alam, R., Ahsan, H., & Khan, S. (2022) · Nutrition Metabolism and Cardiovascular Diseases · doi:10.1016/j.numecd.2022.11.023 · Cited by 32
NAD+ metabolism is a key modulator of bacterial respiratory epithelial infections
Klabunde, B., Wesener, A., Bertrams, W., Beinborn, I., Paczia, N., Surmann, K., Blankenburg, S., Wilhelm, J., Serranía, J., Knoops, K., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-41372-w · Cited by 31
Akbarzadeh, S., Nabipour, I., Jafari, S. M., Movahed, A., Motamed, N., Assadi, M., & Hajian, N. (2011) · Diabetes Research and Clinical Practice · doi:10.1016/j.diabres.2011.10.004 · Cited by 32
Dysregulation of Myeloid‐specific Transcription Factors in Congenital Neutropenia
Skokowa, J., & Welte, K. (2009) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2009.04963.x · Cited by 31
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 40
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
Non coding RNAs as the critical factors in chemo resistance of bladder tumor cells
Zangouei, A. S., Rahimi, H. R., Mojarrad, M., & Moghbeli, M. (2020) · Diagnostic Pathology · doi:10.1186/s13000-020-01054-3 · Cited by 30
Ismaiel, A., Leucuta, D., Popa, S., & Dumitrascu, D. L. (2021) · Journal of Clinical Medicine · doi:10.3390/jcm10143029 · Cited by 30
Nampt affects mitochondrial function in aged oocytes by mediating the downstream effector FoxO3a
Zhuan, Q., Li, J., Du, X., Zhang, L., Meng, L., Cheng, K., Zhu, S., Hou, Y., & Fu, X. (2021) · Journal of Cellular Physiology · doi:10.1002/jcp.30532 · Cited by 29
Design of an in vitro multienzyme cascade system for the biosynthesis of nicotinamide mononucleotide
Zhou, C.-L., Feng, J., Wang, J., Hao, N., Wang, X., & Chen, K. (2022) · Catalysis Science & Technology · doi:10.1039/d1cy01798e · Cited by 31
Rohrbach, S., Aslam, M., Niemann, B., & Schulz, R. (2014) · British Journal of Pharmacology · doi:10.1111/bph.12650 · Cited by 31
Wątroba, M., Maślińska, D., & Maśliński, S. (2012) · Advances in Medical Sciences · doi:10.2478/v10039-012-0039-1 · Cited by 30
McClure, J. M., Wierman, M. B., Maqani, N., & Smith, J. S. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.367524 · Cited by 30
The circadian clock in adult neural stem cell maintenance
Draijer, S., Chaves, I., & Hoekman, M. F. M. (2018) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2018.05.007 · Cited by 31
Imai, S. (2025) · npj Aging · doi:10.1038/s41514-025-00192-6 · Cited by 30
Self-citationA patent review of sirtuin activators: an update
Villalba, J. M., de Cabo, R., & Alcain, F. J. (2012) · Expert Opinion on Therapeutic Patents · doi:10.1517/13543776.2012.669374 · Cited by 29
Mitochondrial Metabolism and Aging in Yeast
Baccolo, G., Stamerra, G., Pellegrino-Coppola, D., Orlandi, I., & Vai, M. (2018) · International review of cytology · doi:10.1016/bs.ircmb.2018.05.001 · Cited by 33
Thejer, B. M., Adhikary, P. P., Teakel, S. L., Fang, J., Weston, P. A., Gurusinghe, S., Anwer, A. G., Gosnell, M. E., Jazayeri, J. A., Ludescher, M., et al. (2020) · BMC Molecular and Cell Biology · doi:10.1186/s12860-020-00268-z · Cited by 29
Poljšak, B., Kovač, V., & Milisav, I. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/8819627 · Cited by 33
NAD+ Homeostasis in Diabetic Kidney Disease
Xu, J., Kitada, M., & Koya, D. (2021) · Frontiers in Medicine · doi:10.3389/fmed.2021.703076 · Cited by 30
NAD+ Metabolism and Diseases with Motor Dysfunction
Lundt, S., & Ding, S. (2021) · Genes · doi:10.3390/genes12111776 · Cited by 27
NMN: The NAD precursor at the intersection between axon degeneration and anti-ageing therapies
Loreto, A., Antoniou, C., Merlini, E., Gilley, J., & Coleman, M. P. (2023) · Neuroscience Research · doi:10.1016/j.neures.2023.01.004 · Cited by 31
Sirtuin biology and relevance to diabetes treatment
Dong, X. C. (2012) · Diabetes Management · doi:10.2217/dmt.12.16 · Cited by 29
α-Lipoic acid as a triglyceride-lowering nutraceutical
Pashaj, A., Xia, M., & Moreau, R. F. (2015) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/cjpp-2014-0480 · Cited by 30
THE CARDIOVASCULAR IMPACT OF VISFATIN - AN INFLAMMATION PREDICTOR BIOMARKER IN METABOLIC SYNDROME
Hognogi, L. D. M., & Vida-Simiti, L. A. (2015) · Medicine and Pharmacy Reports · doi:10.15386/cjmed-591 · Cited by 28
Fukaya, M., Tamura, Y., Chiba, Y., Tanioka, T., Mao, J., Inoue, Y., Yamada, M., Waeber, C., Ido-Kitamura, Y., Kitamura, T., et al. (2013) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2013.11.024 · Cited by 30
Pang, J., Gong, H., Xi, C., Fan, W., Dai, Y., & Zhang, T. (2010) · Journal of Cellular Biochemistry · doi:10.1002/jcb.22919 · Cited by 28
Organ Protection by Caloric Restriction Depends on Activation of the De Novo NAD+ Synthesis Pathway
Späth, M. R., Hoyer-Allo, K. J. R., Seufert, L., Höhne, M., Lucas, C., Bock, T., Isermann, L., Brodesser, S., Lackmann, J., Kiefer, K., et al. (2023) · Journal of the American Society of Nephrology · doi:10.1681/asn.0000000000000087 · Cited by 27
Gouranton, E., Romier, B., Marcotorchino, J., Tourniaire, F., Astier, J., Peiretti, F., & Landrier, J. (2014) · Adipocyte · doi:10.4161/adip.28729 · Cited by 28
Radons (2009) · International Journal of Oncology · doi:10.3892/ijo_00000317 · Cited by 28
Regulative Effect of Nampt on Tumor Progression and Cell Viability in Human Colorectal Cancer
Lv, X., Zhang, L., Zhu, Y., Said, H. M., Shi, J., & Xu, G. (2015) · Journal of Cancer · doi:10.7150/jca.12341 · Cited by 28
Pandya, J. D., Musyaju, S., Modi, H. R., Okada-Rising, S. L., Bailey, Z. S., Scultetus, A. H., & Shear, D. A. (2024) · Journal of Translational Medicine · doi:10.1186/s12967-024-04908-2 · Cited by 33
Gruenbacher, G., Gander, H., Rahm, A., Dobler, G., Drasche, A., Troppmair, J., Nußbaumer, W., & Thurnher, M. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.01870 · Cited by 27
Hypothalamic NAD+-Sirtuin Axis: Function and Regulation
Roh, E., & Kim, M. (2020) · Biomolecules · doi:10.3390/biom10030396 · Cited by 30
Annie, L., Gurusubramanian, G., & Roy, V. K. (2020) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2020.105763 · Cited by 27
Philp, A. M., Butterworth, S., Davis, E. T., & Jones, S. W. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22136719 · Cited by 27
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 30
Regulation of SIRT1 in Ovarian Function: PCOS Treatment
Li, X., He, Y., Wu, S., Zhang, P., Gan, M., Chen, L., Zhao, Y., Niu, L., Zhang, S., Jiang, Y., et al. (2023) · Current Issues in Molecular Biology · doi:10.3390/cimb45030133 · Cited by 29
McGuinness, H. Y., Gu, W., Shi, Y. Y., Kobe, B., & Ve, T. (2023) · The Neuroscientist · doi:10.1177/10738584231162508 · Cited by 29
Katahira, R., & Ashihara, H. (2009) · Planta · doi:10.1007/s00425-009-1023-2 · Cited by 27
EWS-FLI1 confers exquisite sensitivity to NAMPT inhibition in Ewing sarcoma cells
Mutz, C., Schwentner, R., Aryee, D. N. T., Bouchard, E. D. J., Mejia, E. M., Hatch, G. M., Kauer, M. O., Katschnig, A. M., Ban, J., Garten, A., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.14976 · Cited by 27
Pan, J., Zhou, H. K., Zhu, S., Jin-lian, H., Zhao, X., Ding, H., Qin, L., & Pan, Y. (2018) · Journal of Cellular Physiology · doi:10.1002/jcp.27228 · Cited by 27
Ji, C., Cong, R., Wang, Y., Wang, Y., Zhang, Q., Zhou, X., Xing, Q., & Song, N. (2019) · Annals of Translational Medicine · doi:10.21037/atm.2019.11.32 · Cited by 26
Nutrigenetics and nutrigenomics—A personalized approach to nutrition
Ahluwalia, M. K. (2021) · Advances in genetics · doi:10.1016/bs.adgen.2021.08.005 · Cited by 27
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
Microbiota-derived metabolites in inflammatory bowel disease
Guggeis, M. A., Harris, D. M. M., Welz, L., Rosenstiel, P. C., & Aden, K. (2025) · Seminars in Immunopathology · doi:10.1007/s00281-025-01046-9 · Cited by 31
Targeting NAD+ Metabolism to Enhance Radiation Therapy Responses
Lewis, J. E., Singh, N., Holmila, R. J., Sumer, B. D., Williams, N. S., Furdui, C. M., Kemp, M. L., & Boothman, D. A. (2018) · Seminars in Radiation Oncology · doi:10.1016/j.semradonc.2018.10.009 · Cited by 29
The Science Behind NMN-A Stable, Reliable NAD+Activator and Anti-Aging Molecule.
Shade, C. W. (2020) · Europe PMC (PubMed Central) · Cited by 24
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
Circulating blood eNAMPT drives the circadian rhythms in locomotor activity and energy expenditure
Park, J.-W., Roh, E., Kang, G. M., Gil, S. Y., Kim, H. K., Lee, C. H., Jang, W. H., Park, S. E., Moon, S. Y., Kim, S. J., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-37517-6 · Cited by 26
Schulz, C., Paulus, K., & Lehnert, H. (2010) · Results and problems in cell differentiation · doi:10.1007/978-3-642-14426-4_16 · Cited by 26
Metabolic alteration of HepG2 in scaffold‐based 3‐D culture: Proteomic approach
Pruksakorn, D., Lirdprapamongkol, K., Chokchaichamnankit, D., Subhasitanont, P., Chiablaem, K., Svasti, J., & Srisomsap, C. (2010) · PROTEOMICS · doi:10.1002/pmic.201000137 · Cited by 26
Huang, P.-S., Son, J., Abbott, L. C., & Winzer‐Serhan, U. H. (2011) · Neuroscience · doi:10.1016/j.neuroscience.2011.09.007 · Cited by 27
Kato, M., & Lin, S.-J. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.558643 · Cited by 29
hMOF Acetylation of DBC1/CCAR2 Prevents Binding and Inhibition of SirT1
Zheng, H., Yang, L., Peng, L., Izumi, V., Koomen, J. M., Seto, E., & Chen, J. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.00874-13 · Cited by 26
Bai, J., Liao, C., Liu, Y., Qin, X., Chen, J., Qiu, Y., Qin, D., Li, Z., Tu, Z.-C., & Jiang, S. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b00324 · Cited by 26
Penke, M., Schuster, S., Gorski, T., Gebhardt, R., Kieß, W., & Garten, A. (2017) · Lipids in Health and Disease · doi:10.1186/s12944-017-0583-6 · Cited by 26
WldS, Nmnats and axon degeneration-progress in the past two decades
Feng, Y., Yan, T., He, Z., & Zhai, Q. (2010) · Protein & Cell · doi:10.1007/s13238-010-0021-2 · Cited by 24
Sirtuin 1 in rat orthotopic liver transplantation: An IGL-1 preservation solution approach
Pantazi, E. D. (2015) · World Journal of Gastroenterology · doi:10.3748/wjg.v21.i6.1765 · Cited by 26
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
Visfatin as a Promising Marker of Cardiometabolic Risk.
Erten, M. (2021) · Europe PMC (PubMed Central) · doi:10.6515/acs.202109_37(5).20210323b · Cited by 25
Nitrogen-15 dynamic nuclear polarization of nicotinamide derivatives in biocompatible solutions
Peters, J. P., Brahms, A., Janicaud, V., Anikeeva, M., Peschke, E., Ellermann, F., Ferrari, A., Hellmold, D., Held‐Feindt, J., Kim, N.-M., et al. (2023) · Science Advances · doi:10.1126/sciadv.add3643 · Cited by 25
Bennetts, B., Yu, Y., Chen, T., & Parker, M. W. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.327551 · Cited by 25
Molecular cloning and characterization of porcine sirtuin genes
Jin, D., Tan, H., Lei, T., Gan, L., Chen, X., Long, Q., Feng, B., & Yang, Z. (2009) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/j.cbpb.2009.04.004 · Cited by 25
Intrinsic directionality of migrating vascular smooth muscle cells is regulated by NAD+ biosynthesis
Yin, H. R., van der Veer, E., Frontini, M. J., Thibert, V., O’Neil, C. H., Watson, A., Szasz, P., Chu, M. W. A., & Pickering, J. G. (2012) · Journal of Cell Science · doi:10.1242/jcs.110262 · Cited by 24
Visfatin: A Potential Therapeutic Target for Rheumatoid Arthritis
Bao, J., Chen, W., & Wu, L. (2009) · Journal of International Medical Research · doi:10.1177/147323000903700601 · Cited by 25
Zrenner, R. M., & Ashihara, H. (2011) · doi:10.1002/9781119991311.ch5 · Cited by 25
Benjamin, C., & Crews, R. (2024) · Metabolites · doi:10.3390/metabo14060341 · Cited by 25
Olaparib induces browning of in vitro cultures of human primary white adipocytes
Nagy, L., Rauch, B., Balla, N., Ujlaki, G., Kis, G. N., Abdul-Rahman, O., Kristóf, E., Sipos, A., Antal, M., Tóth, A., et al. (2019) · Biochemical Pharmacology · doi:10.1016/j.bcp.2019.06.022 · Cited by 24
Macrophage-stem cell crosstalk: regulation of the stem cell niche
Manneken, J. D., & Currie, P. D. (2023) · Development · doi:10.1242/dev.201510 · Cited by 27
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
Gurd, B. J., & Williams, C. (2012) · The Application of Clinical Genetics · doi:10.2147/tacg.s31276 · Cited by 24
Tsai, P.-J. S., Davis, J. W., Thompson, K. S., & Bryant‐Greenwood, G. D. (2015) · Reproductive Sciences · doi:10.1177/1933719115570908 · Cited by 24
The relationship between visfatin and metabolic syndrome in postmenopausal women
Kim, J., Kim, S.-H., Im, J., & Lee, D. (2010) · Maturitas · doi:10.1016/j.maturitas.2010.05.002 · Cited by 24
NAMPT pathway is involved in the FOXO3a-mediated regulation of GADD45A expression
Thakur, B. K., Lippka, Y., Dittrich, T., Chandra, P., Skokowa, J., & Welte, K. (2012) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.03.017 · Cited by 24
Friebe, D., Löffler, D., Schönberg, M., Bernhard, F., Buttner, P. G., Landgraf, K., Kieß, W., & Körner, A. (2011) · PLoS ONE · doi:10.1371/journal.pone.0019526 · Cited by 24
Li, S., Wang, C., Li, K., Li, L., Tian, M., Xie, J., Yang, M., Jia, Y., He, J., Gao, L., et al. (2016) · Scientific Reports · doi:10.1038/srep26746 · Cited by 24
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
Metadata
- Authors
- Revollo, J. R., Grimm, A. A., & Imai, S.-I.
- Affiliations
- Washington University in St. Louis (US)
- Corresponding author
- Imai, Shin-ichiro
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2004-12
- Volume
- 279
- Issue
- 49
- Pages
- 50754-50763
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2108536847
- Cited by
- 1,010
- References
- 61
- Citations by year
- 2026: 31 · 2025: 34 · 2024: 54 · 2023: 43 · 2022: 52 · 2021: 49 · 2020: 57 · 2019: 51 · 2018: 56 · 2017: 62 · 2016: 48 · 2015: 51 · 2014: 41 · 2013: 58 · 2012: 55
- FWCI
- 9.04
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Ellison Medical Foundation
- Leukemia and Lymphoma Society
- 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
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Keywords
- NAD biosynthesis, visfatin, nicotinamide mononucleotide adenylyltransferase, rate-limiting enzyme, mouse fibroblasts, gene expression profiling, aging
- MeSH terms
- Animals, Cell Differentiation, Chromatography, High Pressure Liquid, Dose-Response Relationship, Drug, Fibroblasts, Fungal Proteins, Kinetics, Luciferases, NAD, Nicotinamide-Nucleotide Adenylyltransferase, Pentosyltransferases, Phylogeny, Recombinant Proteins, Saccharomyces cerevisiae, Transcription, Genetic, Blotting, Western, Gene Library, Cytokines, Genes, Reporter, DNA, Complementary, Reverse Transcriptase Polymerase Chain Reaction, Catalytic Domain, Oligonucleotide Array Sequence Analysis, Sirtuins, NIH 3T3 Cells, Mice, Nicotinamide Phosphoribosyltransferase, Sirtuin 1
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