The NAD Biosynthesis Pathway Mediated by Nicotinamide Phosphoribosyltransferase Regulates Sir2 Activity in Mammalian Cells

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

Normalization for cDNA microarray data: a robust composite method addressing single and multiple slide systematic variation.

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

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

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

The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms

Kaeberlein, 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

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

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

Effects of long‐acting somatostatin analogues on adrenal growth and phosphoribosyl pyrophosphate formation in experimental diabetes

Kunjara, S., Greenbaum, A. L., Sochor, M., Ali, M., Flyvbjerg, A., Grønbæk, H., & McLean, P. (2012) · International Journal of Experimental Pathology · doi:10.1111/j.1365-2613.2011.00801.x · Cited by 5

Ablation of Nampt in AgRP neurons leads to neurodegeneration and impairs fasting‐ and ghrelin‐mediated food intake

de Guia, R. M., Hassing, A. S., Ma, T., Plucińska, K., Holst, B., Gerhart‐Hines, Z., Emanuelli, B., & Treebak, J. T. (2021) · The FASEB Journal · doi:10.1096/fj.202002740r · Cited by 5

Harnessing NAD+ Metabolism as Therapy for Cardiometabolic Diseases

Chakraborty, A. D., Minor, K., Nizami, H. L., Chiao, Y. A., & Lee, C. F. (2022) · Current Heart Failure Reports · doi:10.1007/s11897-022-00550-5 · Cited by 6

Field-based 3D-QSAR studies on amide- and urea-containing NAMPT inhibitors

Özgencil, F., & Eren, G. (2023) · Chemometrics and Intelligent Laboratory Systems · doi:10.1016/j.chemolab.2023.104984 · Cited by 5

Glucose Restriction: Longevity SIRTainly, but without Building Muscle?

Cantó, C., & Auwerx, J. H. (2008) · Developmental Cell · doi:10.1016/j.devcel.2008.04.012 · Cited by 5

Can we use the epigenetic bioactivity of caloric restriction and phytochemicals to promote healthy ageing?

Christodoulou, M. S., Thomas, A., Poulain, S., Vidaković, M., Lahtela-Kakkonen, M. K., Matulis, D., Bertrand, P., Bártová, E., Blanquart, C., Mikros, E., et al. (2014) · MedChemComm · doi:10.1039/c4md00268g · Cited by 6

p53 controls choice between apoptotic and non-apoptotic death following DNA damagePreprint

Honeywell, M. E., Isidor, M. S., Harper, N. W., Fontana, R. E., Cruz‐Gordillo, P., Porto, S. A., Fraser, C. S., Sarosiek, K. A., Guertin, D. A., Spinelli, J. B., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.01.17.524444 · Cited by 6

Multi-omics Characterization of Acquired Olaparib Resistance in BRCA1 and BRCA2 Mutant Breast Cancer Cell Lines

Anagho, H. A., Mullari, M., Mattanovich, M., Cho, H., Pedersen, A.-K., Palasca, O., Olsen, J. V., Locard‐Paulet, M., & Nielsen, M. L. (2025) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2025.101034 · Cited by 5

A metabolic constraint in de novo NAD+ synthesis drives mucosal inflammation in IBD

Wehkamp, L., Harris, D. M. M., Kim, N., Alsaadi, A. I., Wu, Q., Oumari, M., Taubenheim, J., Volk, V., Credidio, G., Koncina, E., et al. (2026) · Journal of Crohn s and Colitis · doi:10.1093/ecco-jcc/jjag043 · Cited by 10

Nanoformulations-based functionalized boron nitride nanosheets delivering nicotinamide mononucleotide with enhanced in vitro anti-aging properties

AbouAitah, K., Turk, A., Bu, Y., Sabbagh, F., Lee, M. K., & Kim, B. S. (2025) · Journal of Drug Delivery Science and Technology · doi:10.1016/j.jddst.2025.106846 · Cited by 5

Need for NAD+: Focus on Striated Muscle Laminopathies

Cardoso, D., & Muchir, A. (2020) · Cells · doi:10.3390/cells9102248 · Cited by 5

Extracellular Nampt (eNampt/Visfatin/PBEF) directly and indirectly stimulates ACTH and CCL2 protein secretion from isolated rat corticotropes

Celichowski, P., Jopek, K., Szyszka, M., Milecka, P., Tyczewska, M., Sakhanova, S., Szaflarski, W., Malendowicz, L. K., & Ruciński, M. (2021) · Advances in Clinical and Experimental Medicine · doi:10.17219/acem/136172 · Cited by 4

Sirtuin 1 as a potential biomarker of undernutrition in the elderly: a narrative review

Kujawowicz, K., Mirończuk-Chodakowska, I., & Witkowska, A. M. (2023) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2023.2214208 · Cited by 4

Efficient Conversion of Nicotinamide Mononucleotide Based on Elucidation of the Limitations in Multienzyme Cascade Reactions

Yu, F., Li, H., Li, X., Shi, J., Feng, Y., & Xue, S. (2025) · Biotechnology Journal · doi:10.1002/biot.202400707 · Cited by 4

The Proposed Effects of Nicotinamide Adenine Dinucleotide (NAD) Supplementation on Energy Metabolism

French, B. D. (2015) · Cited by 4

Molecular correlates of MRS‐based 31phosphocreatine muscle resynthesis rate in healthy adults

Darpolor, M. M., Singh, M., Covington, J. D., Hanet, S., Ravussin, É., & Carmichael, O. T. (2020) · NMR in Biomedicine · doi:10.1002/nbm.4402 · Cited by 4

Deletion of Nmnat1 in Skeletal Muscle Leads to the Reduction of NAD+ Levels but Has No Impact on Skeletal Muscle Morphology and Fiber Types

Karim, M., Iqbal, T., Nawaz, A., Yaku, K., & Nakagawa, T. (2023) · Journal of Nutritional Science and Vitaminology · doi:10.3177/jnsv.69.184 · Cited by 4

Pre-B cell colony-enhancing factor in lower vertebrates: First evidence of this cytokine being involved in antioxidant activity by reconstruction of a novel NAD salvage pathway in E. coli

Dong, W.-R., Xiang, L., & Shao, J. (2008) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2008.10.007 · Cited by 4

Resistin, visfatin and insulin sensitivity in selected phases of annual training cycle of triathletes

Śliwicka, E., Pilaczyńska-Szczȩśniak, Ł., Nowak, A., & Zieliński, J. (2012) · Acta Physiologica Hungarica · doi:10.1556/aphysiol.99.2012.1.6 · Cited by 4

Respected Sir(2): magic target for diabetes.

Nerurkar, P. V., & Nerurkar, V. R. (2008) · PubMed · Cited by 4

The assessment of an in-vitro model for evaluating the role of PARP in ethanol-mediated hepatotoxicity

Harbison, R., Coyle, J., Mayo-PEREZ, A., Bourgeois, M., Johnson, G., & Morris, S. (2015) · International Journal of Critical Illness and Injury Science · doi:10.4103/2229-5151.152300 · Cited by 4

The Relationship between Plasma Visfatin/Nampt and Type 2 Diabetes, Obesity, Insulin Resistance, and Cardiovascular Disease

Brema, I. A. (2016) · Endocrinology&Metabolism International Journal · doi:10.15406/emij.2016.03.00068 · Cited by 4

Interplay Between Nutrient-Sensing Molecules During Aging and Longevity

Hadem, I. K. H., Majaw, T., & Sharma, R. (2020) · Springer eBooks · doi:10.1007/978-981-32-9005-1_18 · Cited by 4

Progress in understanding how clock genes regulate aging and associated metabolic processes

Su, Y., Wang, M., Chen, J., Bao, Y., Wen, R., Ren, H., & Luan, Z. (2025) · Frontiers in Physiology · doi:10.3389/fphys.2025.1654369 · Cited by 4

NAMPT modulates muscle fiber type transition in PAD myopathy via the cGMP-PKG signaling pathway

Yang, Q., Shi, Y., Li, W., Xiong, X., Chen, Q., & Zheng, M. (2025) · Biology Direct · doi:10.1186/s13062-025-00705-z · Cited by 3

Utility of Extracellular Nicotinamide Phosphoribosyl Transferase as a Novel Biomarker in Predicting Early Severe Organ Dysfunction and Mortality in Acute Respiratory Distress Syndrome: A Prospective Observational Study

Rao, S., Srinivas, T., Vishwas, P., Todur, P., Udupa, A. A., Rao, S., & Chaudhuri, S. (2025) · Indian Journal of Critical Care Medicine · doi:10.5005/jp-journals-10071-25092 · Cited by 3

Exosomal NAMPT from Engineered Mesenchymal Stem Cells Mitigates Aortic Stenosis via Metabolic and Anti-Inflammatory Pathways

Kundu, D. K., Kiedrowski, M. J., Gadd, J., Gao, M., Evan, M., Wang, Y., Yin, L., Ohanyan, V. A., Chilian, W. M., & Dong, F. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms27010256 · Cited by 3

Regulatory effect and mechanism of CircSEC24A in IL-1β-induced osteoarthritis

Wang, Y., Chen, X., Chen, Y., Sun, Q., & Wang, H. (2024) · Archives of Physiology and Biochemistry · doi:10.1080/13813455.2024.2404975 · Cited by 3

The Role of Visfatin in Gastric and Esophageal Cancer: From Biomarker to Therapeutic Target

Mylonakis, A., Kozadinos, A., Frountzas, M., Kapetanakis, E. I., Lidoriki, I., Despotidis, M., Karanikki, E., Triantafyllou, T., Theodorou, D. A., Toutouzas, K. G., et al. (2025) · Cancers · doi:10.3390/cancers17081377 · Cited by 3

Advances in Relationship Between Deacetylase (Sirtuin) and Aging

Qi, P. E. N. G., Chen, W., & Liu, X. (2011) · PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS · doi:10.3724/sp.j.1206.2010.00241 · Cited by 3

The Role of NAD+ in Anti-Aging Therapies

Huang, T. (2019) · American Journal of Biomedical Science & Research · doi:10.34297/ajbsr.2019.06.001080 · Cited by 3

Possible Therapeutic Potential of Flavonoids and Phenolic Acids from Honey in Age-Related Neurodegenerative Diseases Via Targeting NAD+ Degradation

Khan, A., Alshahrani, S., Arafah, A. M., Qamar, W., Shoaib, A., Wali, A. F., Amin, I., Alqahtani, S. S., & Rehman, M. U. (2020) · Springer eBooks · doi:10.1007/978-981-15-7305-7_2 · Cited by 3

NAD+: a crucial regulator of sirtuin activity in aging

Braidy, N., & Villalva, M. D. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-814118-2.00008-2 · Cited by 4

+Sirtuins as NAD

Kumar, A., & Dvir‐Ginzberg, M. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-823928-5.00028-1 · Cited by 3

Nicotinamide phosphoribosyltransferase regulates the cell differentiation and mineralization in cultured odontoblasts

Kang, K., Kim, J., Seo, J.-Y., Lim, H., Kim, T., Yu, S., Kim, H., Kim, C. S., Chun, H. S., Park, J., et al. (2021) · Korean Journal of Physiology and Pharmacology · doi:10.4196/kjpp.2022.26.1.37 · Cited by 3

Plasma-activated medium exerts tumor-specific inhibitory effect on hepatocellular carcinoma via disruption of the salvage pathway

Bai, Y., Dai, C., Chen, N., Zhou, X., Li, H., Xu, Q., & Xu, Y. (2024) · Journal of Clinical Biochemistry and Nutrition · doi:10.3164/jcbn.23-112 · Cited by 3

SIRT1 in Metabolic Health and Disease

Boutant, M., & Cantó, C. (2016) · Springer eBooks · doi:10.1007/978-94-024-0962-8_4 · Cited by 3

Rola sirtuin w naprawie DNA

Kciuk, M., & Kontek, R. (2020) · Postępy Biochemii · doi:10.18388/pb.2020_319 · Cited by 3

Enhance Trial: Effects of NAD3® on Hallmarks of Aging and Clinical Endpoints of Health in Middle Aged Adults: A Subset Analysis Focused on Blood Cell NAD+ Concentrations and Lipid Metabolism

Roberts, M. D., Osburn, S. C., Godwin, J. S., Ruple, B. A., Monica, M. B. L., Raub, B. J., Sandrock, J. E., Ziegenfuss, T. N., & Lopez, H. L. (2022) · Physiologia · doi:10.3390/physiologia2010002 · Cited by 3

Adenosine and Other Purinergic Products in Circadian Timing

Muheim, C., & Brown, S. A. (2012) · Springer eBooks · doi:10.1007/978-1-4614-3903-5_11 · Cited by 4

Mitochondrial sirtuins in the rat adrenal gland: location within the glands of males and females, hormonal and developmental regulation of gene expressions

Celichowski, P., Jopek, K., Szyszka, M., Tyczewska, M., Malendowicz, L. K., & Ruciński, M. (2017) · Folia Histochemica et Cytobiologica · doi:10.5603/fhc.a2017.0020 · Cited by 3

Mechanism of Nampt gene expression regulation

Huang, R., Zi-Ru, W. A. N. G., Sun, Y. N., Zhang, G., & Lü, Y.-P. (2012) · Hereditas (Beijing) · doi:10.3724/sp.j.1005.2012.01561 · Cited by 3

Spatial heterogeneity of glioblastoma cells reveals sensitivity to NAD + depletion at tumor edgePreprint

Yamashita, D., Botta, D., Cho, H. J., Guo, X., Ozaki, S., Flanary, V. L., Sirota, I., Gao, M., Yamaguchi, S., Nakano, M. A., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.11.26.399725 · Cited by 2

Mitochondrial Function and Neurodegenerative Diseases

Wilkins, H. M., Weidling, I., Koppel, S., Wang, X., von Schulze, A., & Swerdlow, R. H. (2018) · The Molecular and Cellular Basis of Neurodegenerative Diseases · doi:10.1016/b978-0-12-811304-2.00013-4 · Cited by 2

Mapping Genetic Modifiers of Polyp Formation in Smad4-Deficient Juvenile Polyposis Using the Collaborative Cross Mouse Population

Zohud, O., Midlej, K., Lone, I. M., Nashef, A., Abu-Elnaaj, I., & Iraqi, F. A. (2026) · Cells · doi:10.3390/cells15100853 · Cited by 2

Nicotinamide Mononucleotide Alleviates Angiotensin II-Induced Human Aortic Smooth Muscle Cell Senescence in a Microphysiological Model

Yin, X., Abudupataer, M., Yang, M., Xiang, B., Lai, H., Wang, C., Li, J., & Zhu, K. (2023) · Journal of Cardiovascular Pharmacology · doi:10.1097/fjc.0000000000001400 · Cited by 2

Novel Calcium-Binding Motif Stabilizes and Increases the Activity of Aspergillus fumigatus Ecto-NADase

Ferrario, E., Kallio, J. P., Strømland, Ø., & Ziegler, M. (2023) · Biochemistry · doi:10.1021/acs.biochem.3c00360 · Cited by 2

Serum Visfatin Level in Psoriasis Patients: A Case-Control Study

Minh, V. N., Chau, N. N. Q., Trinh, H. K. T., & Ngo, H. X. (2024) · The Open Dermatology Journal · doi:10.2174/0118743722311288240509113308 · Cited by 2

CircABHD2 Inhibits Malignant Progression of Endometrial Cancer by Regulating NAD+/NAMPT Metabolism Axis

Li, H., Xu, H., Liu, M., Li, Y., Yuan, S., Yin, P., Gong, Z., & Zhong, S. (2024) · Molecular Biotechnology · doi:10.1007/s12033-024-01226-2 · Cited by 3

Dieta hipocalórica y longevidad

Angosto, M. C. (2009) · Anales de la Real Academia Nacional de Farmacia · Cited by 2

Aging Kidney: Modern Perspectives for an ‘Old’ Problem

Grosjean, F., Vlassara, H., & Striker, G. E. (2011) · Aging Health · doi:10.2217/ahe.11.63 · Cited by 2

Cloning, Expression and Characterization of Mouse (Mus musculus) Nicotinamide 5-Mononucleotide Adenylyltransferase-2

Raches, D. W., Xiao, S., Kusumanchi, P., Yalowitz, J. A., Sanghani, P. C., Long, E. C., Antony, A. C., & Jayaram, H. N. (2011) · Medicinal Chemistry · doi:10.2174/157340611797928262 · Cited by 2

Nmnat1-Rbp7 Is a Conserved Fusion-Protein That Combines NAD+ Catalysis of Nmnat1 with Subcellular Localization of Rbp7

Chen, H., Babino, D., Schönbichler, S. A., Arkhipova, V., Töchterle, S., Martin, F., Huck, C. W., Lintig, J. V., & Meyer, D. (2015) · PLoS ONE · doi:10.1371/journal.pone.0143825 · Cited by 2

Expression, purification, and enzymatic activity assay of nicotinamide mononucleotide adenylyltransferase: Expression, purification, and enzymatic activity assay of nicotinamide mononucleotide adenylyltransferase

Lu, X.-Q., Zhang, R.-Y., Xu, X.-W., Guang, Y., & Miao, C.-Y. (2010) · Academic Journal of Second Military Medical University · doi:10.3724/sp.j.1008.2010.01251 · Cited by 2

High-Intensity Exercise and Carbohydrate Supplementation do not Alter Plasma Visfatin.

Mellick, P. F., Feger, B. J., Oberlin, D. J., Davis, P. G., & Wideman, L. (2017) · PubMed Central · Cited by 2

Sirtuin Deacetylases: Linking Mycobacterial Infection and Host Metabolism

Smulan, L. J., Kornfeld, H., & Singhal, A. (2020) · Springer eBooks · doi:10.1007/978-3-030-56905-1_2 · Cited by 2

Metabolic Regulation of Lysine Acetylation: Implications in Cancer

Singh, S., Senapati, P., & Kundu, T. K. (2022) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-031-07634-3_12 · Cited by 2

Effect of NAMPT on the proliferation and apoptosis in odontoblast-like MDPC-23 cell

Kang, Y.-R., Park, J., Kim, C. S., Kim, H., Yu, S., Chun, H. S., Lim, H., Seo, J.-Y., Kim, J., & Kim, D. K. (2024) · Cellular and Molecular Biology · doi:10.14715/cmb/2024.70.3.4 · Cited by 2

Sirtuins as Metabolic Modulators of Muscle Plasticity

Menzies, K. J., Zaldivar‐Jolissaint, J. F., & Auwerx, J. H. (2016) · Springer eBooks · doi:10.1007/978-94-024-0962-8_9 · Cited by 2

Regulation of Sirtuins by Systemic NAD + Biosynthesis

Yoshida, M., & Imai, S. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-813499-3.00002-2 · Cited by 3

Naturalne i syntetyczne modulatory aktywności sirtuin

Wiercińska, M., & Rosołowska‐Huszcz, D. (2017) · Cited by 2

The influence of visfatin and visfatin gene polymorphisms on glucose and obesity-related phenotypes and their responses to aerobic exercise training

McKenzie, J. A. (2008) · University Libraries (University of Maryland) · Cited by 2

Molecular physiological studies on health effects of dietary nicotinamide riboside, a vitamin B3

Shi, W. (2019) · doi:10.18174/471911 · Cited by 2

Pyridine Nucleotide Cycle

Ashihara, H., Ludwig, I. A., & Crozier, A. (2020) · doi:10.1002/9781119476139.ch19 · Cited by 2

NNMT promotes tubular senescence and fibrosis in chronic kidney diseasePreprint

Chanvillard, L., Lantermans, H. C., Wall, C., Thévenet, J., Butter, L. M., Tauzin, L., Claessen, N., Christen, S., Karaz, S., Lassueur, S., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.01.06.631437 · Cited by 2

Trimetazidine with an adjuvant therapy to normalize the circulating visfatin concentration: Future perspective and mechanistic strategies

Maheswari, G. U., Yamini, B., Guru, A., Velayutham, M., Dhandapani, V. E., Karuppiah, K. M., & Amalorpavanaden, N. D. (2023) · Journal of King Saud University - Science · doi:10.1016/j.jksus.2023.102950 · Cited by 1

Thiophenyl Derivatives of Nicotinamide Are Metabolized by the NAD Salvage Pathway into Unnatural NAD Derivatives That Inhibit IMPDH and Are Toxic to Peripheral Nerve Cancers

Theodoropoulos, P. C., Guo, H. H., Wang, W., Crossley, E., Rivera‐Cancel, G., Fang, M., Nguyen, T. H., Baniasadi, H. R., Williams, N. S., Ready, J. M., et al. (2024) · ACS Chemical Biology · doi:10.1021/acschembio.4c00170 · Cited by 1

Identification of Ferroptosis-Associated Genes in Primary Open-Angle Glaucoma through Bioinformatics Analysis

Hong, D. (2025) · Critical Reviews in Eukaryotic Gene Expression · doi:10.1615/critreveukaryotgeneexpr.2025057767 · Cited by 1

PPDPF: Preventing kidney disease through NAD + regulation

Imai, S. (2025) · Science Advances · doi:10.1126/sciadv.adw6815 · Cited by 1

Neuronal C/EBPβ Shortens the Lifespan via Inactivating NAMPT

Li, B., Xie, Z., Wang, M., Nie, S., Qian, Z., Meng, X., Liu, X., Kang, S. S., & Ye, K. (2025) · Advanced Science · doi:10.1002/advs.202414871 · Cited by 3

NAD+ and Its Precursors for Health and Longevity

Yi, L. (2026) · Healthy ageing and longevity · doi:10.1007/978-3-032-11608-6_5 · Cited by 1

Emerging chemical strategies for CD38 inhibition: restoring NAD+ metabolism and disease control

Zhang, Z., Ansari, A. J., Fayne, E., & Zhang, Y. (2026) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2026.118676 · Cited by 1

Skin Cancer Prevention and Antiaging: Role of Nicotinamide

Moro, F., Panebianco, A., Bartolocci, V., Capone, A., Guardo, A. D., Hyeraci, M., Gemma, G. P. A., Lella, G. D., Colonna, L., Ricci, F., et al. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27114918 · Cited by 1

SIRT1: Protean roles at the nexus of health, disease, and therapeutics

Chaqour, B. (2026) · Journal of Cell Communication and Signaling · doi:10.1002/ccs3.70086 · Cited by 1

Pyrroloquinoline Quinone and NAD+ Metabolism in Glaucoma: A Molecular Rationale for Combined Neuroprotection

Medoro, A., Davinelli, S., Mazzotta, C. G., Agnifili, L., & Scapagnini, G. (2026) · Pharmaceuticals · doi:10.3390/ph19081268 · Cited by 1

In silico screening of candidate NAMPT modulators for treatment of age-related diseases

Nahálková, J., & Zanchi, F. B. (2026) · In Silico Research in Biomedicine · doi:10.1016/j.insi.2026.100587 · Cited by 1

Regeneration and Aging: Regulation by Sirtuins and the NAD+ Salvage Pathway

Borradaile, N. M., Watson, A., & Pickering, J. G. (2010) · Elsevier eBooks · doi:10.1016/b978-0-12-380928-5.10019-3 · Cited by 3

Nicotinamide Phosphoribosyltransferase Inhibitors

Wu, D., Cheranova, D. I., Daniel, P., Qin, L., & Qing, S. (2012) · InTech eBooks · doi:10.5772/34981 · Cited by 1

Toward Productive Aging: SIRT1, Systemic NAD Biosynthesis, and the NAD World

Imai, S. (2010) · Cornea · doi:10.1097/ico.0b013e3181ea4714 · Cited by 1

Nutrient Sensors Regulating Peptides

Çakır, I., & Nillni, E. A. (2018) · Springer eBooks · doi:10.1007/978-3-319-89506-2_6 · Cited by 1

Non-cell autonomous effect of neuronal nicotinamide phosphoribosyl transferase on the function of neuromuscular junctions

Lundt, S., & Ding, S. (2020) · Neural Regeneration Research · doi:10.4103/1673-5374.290893 · Cited by 1

Plasma Visfatin is reduced in Subjects with the Metabolic Syndrome and Pre-Diabetes

(2018) · doi:10.31038/edmj.2018234 · Cited by 1

Influence of the storage duration on the health promoting tyrosine, tryptophan, and total phenolics in potato tubers

Asakavičiūtė, R., & Maknickienė, Z. (2024) · Czech Journal of Food Sciences · doi:10.17221/161/2023-cjfs · Cited by 1

Neuroprotective Effect of 7,8-dihydroxyflavone in a Mouse Model of HIV-Associated Neurocognitive Disorder (HAND)

Makar, T. K., Joseph, B., Bosung, S., Keledjian, K. M., Davis, H., Ghosh, M., Koirala, A., Ishani, G., Shreya, M., Heredia, A., et al. (2024) · Journal of Neuroscience and Neurological Disorders · doi:10.29328/journal.jnnd.1001101 · Cited by 1

Advances in Sirtuin on The Mechanism of Calorie Restriction on Lifespan*

Liu, B., Chen, W., Liu, X., & Zhou, Z. (2012) · PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS · doi:10.3724/sp.j.1206.2011.00146 · Cited by 1

Biochemistry and Enzymology of Sirtuins

Yang, Y. J., & Sauve, A. A. (2016) · Springer eBooks · doi:10.1007/978-94-024-0962-8_1 · Cited by 1

The Role of Vistafin in Diabetes-Induced Impairment of Endothelial Repair System

Berezin, A. Е. (2017) · Translational Biomedicine · doi:10.21767/2172-0479.1000104 · Cited by 1

Computational model of circadian oscillator in mammals: Interaction with NAD+/SIRT1 system and age-related changes in the expression of circadian oscillator genes

Podkolodnyy, N. L., Tverdokhleb, N. N., & Podkolodnaya, O. A. (2017) · Russian Journal of Genetics Applied Research · doi:10.1134/s2079059717050161 · Cited by 1

Nampt (Visfatin) Influence on Proliferative Activity of Normal Rat Adrenocortical Cells and Human Adrenal Corticocarcinoma Nci-H295r Cells

Celichowski, P., Jopek, K., Szyszka, M., Milecka, P., Malendowicz, L. K., Tyczewska, M., & Ruciński, M. (2018) · Medical Journal of Cell Biology · doi:10.2478/acb-2018-0007 · Cited by 1

Drosophila Nicotinamidase And Sir2 In Longevity Regulation And Oxidative Stress Response, And The Implications For Aging Theory

Miller, G. S. (2010) · Human Biology · Cited by 1

NAD‐Dependent Deacetylases as Therapeutic Targets

Li, H., Simon, J. A., & Bedalov, A. (2009) · Methods and principles in medicinal chemistry · doi:10.1002/9783527627073.ch10 · Cited by 1

Functional analysis of mitochondrial sirtuins in C. elegans and mammalian cells

Wirth, M. (2011) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-3229 · Cited by 1

REGULATION OF TRANSLATION AND TRANSCRIPTION BY SIRT1: POTENTIAL NOVEL MECHANISMS FOR REGULATING STRESS RESPONSE AND AGING

Ghosh, H. S. (2007) · D-Scholarship@Pitt (University of Pittsburgh) · Cited by 1

Sirtuin Function in Longevity

Smith, D. L., & Smith, J. S. (2009) · Springer eBooks · doi:10.1007/978-90-481-3465-6_6 · Cited by 1

Circadian Clock, Epigenetic Regulators (Sirtuins), and Metabolism

Meyer‐Ficca, M. L., & Meyer, R. G. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-801238-3.65831-2 · Cited by 1

Promoting healthy ageing

Connell, N. J. (2021) · Research Publications (Maastricht University) · doi:10.26481/dis.20210122nc · Cited by 1

Synthetic lethality between CCNE1 hyperactivity and PARG inhibition in breast cancerPreprint

Bandyopadhyay, S., Hu, H.-M., & Jacobo, M. J. (2022) · Research Square · doi:10.21203/rs.3.rs-2231840/v1 · Cited by 1

Etude de la biosynthese du nad chez les plantes : conséquences physiologiques de sa manipulation chez Arabidopsis thaliana

Pétriacq, P. (2011) · doi:10.70675/425cd534zc198z4892z9eefzfc5d8187c926 · Cited by 1

The role of CD38 expression on NAD levels and cell physiology in a leukaemia model

Al-Abady, Z. N. (2013) · PEARL (University of Plymouth) · doi:10.13140/rg.2.2.34066.66249

Regulation of neutrophil function by NAMPT

Roberts, K. (2013) · doi:10.17638/00008355

Stability of nicotinamide - adenine dinucleotide phosphate and nicotinamide - adenine dinucleotide in tissue extracts under mildly acidic conditions

Neubert, D., Schulz, H.-U., & Hoehne, R. (1964) · Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects · doi:10.1016/0926-6569(64)90023-9 · Cited by 9

The regulation of nicotinamide adenine dinucleotide biosynthesis by Nampt/PBEF/visfatin in mammals

Revollo, J. R., Grimm, A. A., & Imai, S. (2007) · Current Opinion in Gastroenterology · doi:10.1097/mog.0b013e32801b3c8f · Cited by 316

Nicotinamide adenine dinucleotide, a metabolic regulator of transcription, longevity and disease

Lin, S.-J., & Guarente, L. (2003) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(03)00006-1 · Cited by 486

Enzymes in the NAD+ Salvage Pathway Regulate SIRT1 Activity at Target Gene Promoters

Zhang, T., Berrocal, J. G., Frizzell, K. M., Gamble, M. J., DuMond, M. E., Krishnakumar, R., Yang, T., Sauve, A. A., & Kraus, W. L. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.016469 · Cited by 234

NAMPT in Regulated NAD Biosynthesis and its Pivotal Role in Human Metabolism

Burgos, E. S. (2011) · Current Medicinal Chemistry · doi:10.2174/092986711795590101 · Cited by 74