Flavonoid Apigenin Is an Inhibitor of the NAD+ase CD38

The metabolic syndrome

Eckel, R. H., Alberti, K., Grundy, S. M., & Zimmet, P. (2010) · The Lancet · doi:10.1016/s0140-6736(09)61794-3 · Cited by 6,283 · see citing works

The metabolic syndrome

Eckel, R. H., Grundy, S. M., & Zimmet, P. (2005) · The Lancet · doi:10.1016/s0140-6736(05)66378-7 · Cited by 5,566 · see citing works

Prevalence of overweight and obesity among US children, adolescents, and adults, 1999-2002.

Hedley, A. A., Ogden, C., Johnson, C. L., Carroll, M., Curtin, L. R., & Flegal, K. (2004) · Journal of the American Medical Association (JAMA) · doi:10.1001/jama.291.23.2847 · Cited by 4,670 · see citing works

Global nutrition transition and the pandemic of obesity in developing countries

Popkin, B. M., Adair, L. S., & Ng, S. W. (2012) · Nutrition Reviews · doi:10.1111/j.1753-4887.2011.00456.x · Cited by 4,313 · see citing works

Resveratrol improves health and survival of mice on a high-calorie diet

Baur, J. A., Pearson, K. J., Price, N. L., Jamieson, H. A., Lerin, C., Kalra, A., Prabhu, V. V., Allard, J. S., Lopez-Lluch, G., Lewis, K., et al. (2006) · Nature · doi:10.1038/nature05354 · Cited by 4,290 · see citing works

Small 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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 2,653 · see citing works

The many roles of histone deacetylases in development and physiology: implications for disease and therapy

Haberland, M., Montgomery, R. L., & Olson, E. N. (2008) · Nature Reviews Genetics · doi:10.1038/nrg2485 · Cited by 2,541 · see citing works

D IETARY F LAVONOIDS : Bioavailability, Metabolic Effects, and Safety

Ross, J. A., & Kasum, C. M. (2002) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.22.111401.144957 · Cited by 2,153 · see citing works

Mammalian Sirtuins: Biological Insights and Disease Relevance

Haigis, M. C., & Sinclair, D. A. (2010) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev.pathol.4.110807.092250 · Cited by 2,085 · see citing works

Small molecule activators of SIRT1 as therapeutics for the treatment of type 2 diabetes

Milne, J. C., Lambert, P. D., Schenk, S., Carney, D. P., Smith, J. J., Gagne, D. J., Jin, L., Boss, O., Perni, R. B., Vu, C. B., et al. (2007) · Nature · doi:10.1038/nature06261 · Cited by 1,707 · see citing works

SIRT1 is required for AMPK activation and the beneficial effects of resveratrol on mitochondrial function

Price, N. L., Gomes, A. P., Ling, A. J. Y., Duarte, F. V., Martin-Montalvo, A., North, B. J., Agarwal, B., Ye, L., Ramadori, G., Teodoro, J. S., et al. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.04.003 · Cited by 1,602 · see citing works

Nicotinamide Mononucleotide, a Key NAD+ Intermediate, Treats the Pathophysiology of Diet- and Age-Induced Diabetes in Mice

Yoshino, J., Mills, K. F., Yoon, M. J., & Imai, S.-I. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.08.014 · Cited by 1,340 · see citing works

The Metabolic Syndrome

Grundy, S. M. (2010) · Springer eBooks · doi:10.1007/978-1-4419-5839-6_1 · Cited by 1,225 · see citing works

Mechanism of Human SIRT1 Activation by Resveratrol

Borra, M. T., Smith, B. C., & Denu, J. M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501250200 · Cited by 1,065 · see citing works

Poly(ADP)-Ribose Polymerase Inhibition: Frequent Durable Responses in BRCA Carrier Ovarian Cancer Correlating With Platinum-Free Interval

Fong, P. C. C., Yap, T. A., Boss, D. S., Carden, C. P., Mergui‐Roelvink, M., Gourley, C., Grève, J. D., Lubiński, J., Shanley, S., Messiou, C., et al. (2010) · Journal of Clinical Oncology · doi:10.1200/jco.2009.26.9589 · Cited by 1,009 · see citing works

Sirt1 protects against high-fat diet-induced metabolic damage

Pfluger, P. T., Herranz, D., Velasco-Miguel, S., Serrano, M., & Tschöp, M. H. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0802917105 · Cited by 928 · see citing works

SRT1720, SRT2183, SRT1460, and resveratrol are not direct activators of SIRT1

Pacholec, M., Bleasdale, J. E., Chrunyk, B., Cunningham, D., Flynn, D., Garofalo, R. S., Griffith, D., Griffor, M., Loulakis, P., Pabst, B., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.088682 · Cited by 915 · see citing works

PARP-1 inhibition increases mitochondrial metabolism through SIRT1 activation

Bai, P., Cantó, C., Oudart, H., Brunyánszki, A., Cen, Y., Thomas, C., Yamamoto, H., Huber, A., Kiss, B., Houtkooper, R. H., et al. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.03.004 · Cited by 837 · see citing works

Polyphenols Stimulate AMP-Activated Protein Kinase, Lower Lipids, and Inhibit Accelerated Atherosclerosis in Diabetic LDL Receptor–Deficient Mice

Zang, M., Xu, S., Maitland, K. A., Zuccollo, A., Hou, X., Jiang, B., Wierzbicki, M., Verbeuren, T. J., & Cohen, R. A. (2006) · Diabetes · doi:10.2337/db05-1188 · Cited by 663 · see citing works

Fasting-dependent glucose and lipid metabolic response through hepatic sirtuin 1

Rodgers, J. T., & Puigserver, P. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0702509104 · Cited by 549 · see citing works

Regulation of intracellular levels of NAD: A novel role for CD38

Aksoy, P., White, T. A., Thompson, M., & Chini, E. N. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.05.042 · Cited by 353 · see citing works

Sirtuins mediate mammalian metabolic responses to nutrient availability

Chalkiadaki, A., & Guarente, L. (2012) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2011.225 · Cited by 342 · see citing works

Hepatic overexpression of SIRT1 in mice attenuates endoplasmic reticulum stress and insulin resistance in the liver

Li, Y., Xu, S., Giles, A. J., Nakamura, K., Lee, J. W., Hou, X., Dönmez, G., Li, J., Luo, Z., Walsh, K., et al. (2011) · The FASEB Journal · doi:10.1096/fj.10-173492 · Cited by 298 · see citing works

The enzyme CD38 (a NAD glycohydrolase, EC 3.2.2.5) is necessary for the development of diet‐induced obesity

Barbosa, M. T., Soares, S. M., Novak, C. M., Sinclair, D. A., Levine, J. A., Aksoy, P., & Chini, E. N. (2007) · The FASEB Journal · doi:10.1096/fj.07-8290com · Cited by 249 · see citing works

Lack of SIRT1 (Mammalian Sirtuin 1) Activity Leads to Liver Steatosis in the SIRT1+/− Mice: A Role of Lipid Mobilization and Inflammation

Xu, F. L., Gao, Z., Zhang, J., Rivera, C. A., Yin, J., Weng, J., & Ye, J. (2010) · Endocrinology · doi:10.1210/en.2009-1013 · Cited by 221 · see citing works

Anti-inflammatory mechanisms of apigenin: inhibition of cyclooxygenase-2 expression, adhesion of monocytes to human umbilical vein endothelial cells, and expression of cellular adhesion molecules

Lee, J., Zhou, H. Y., Cho, S. Y., Kim, Y. S., Lee, Y. S., & Jeong, C. S. (2007) · Archives of Pharmacal Research · doi:10.1007/bf02980273 · Cited by 220 · see citing works

Inhibition of ultraviolet light induced skin carcinogenesis in SKH-1 mice by apigenin, a plant flavonoid.

Birt, D. F., Mitchell, D. L., Gold, B. I., Pour, P. M., & Pinch, H. C. (1997) · PubMed · Cited by 201 · see citing works

Deleted in breast cancer–1 regulates SIRT1 activity and contributes to high-fat diet–induced liver steatosis in mice

Escande, C., Chini, C. C. S., Nin, V., Dykhouse, K. M., Novak, C. M., Levine, J. A., van Deursen, J., Gores, G. J., Chen, J., Lou, Z., et al. (2010) · Journal of Clinical Investigation · doi:10.1172/jci39319 · Cited by 186 · see citing works

Regulation of SIRT 1 mediated NAD dependent deacetylation: A novel role for the multifunctional enzyme CD38

Aksoy, P., Escande, C., White, T. A., Thompson, M., Soares, S. M., Benech, J. C., & Chini, E. N. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.08.066 · Cited by 173 · see citing works

Treatment with SRT1720, a SIRT1 activator, ameliorates fatty liver with reduced expression of lipogenic enzymes in MSG mice

Yamazaki, Y., Usui, I., Kanatani, Y., Matsuya, Y., Tsuneyama, K., Fujisaka, S., Bukhari, A., Suzuki, H., Senda, S., Imanishi, S., et al. (2009) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.90997.2008 · Cited by 164 · see citing works

Mitochondrial Localization of PARP-1 Requires Interaction with Mitofilin and Is Involved in the Maintenance of Mitochondrial DNA Integrity

Rossi, M. N., Carbone, M., Mostocotto, C., Mancone, C., Tripodi, M., Maione, R., & Amati, P. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.025882 · Cited by 163 · see citing works

Poly(ADP-Ribose) Polymerase Inhibition: “Targeted” Therapy for Triple-Negative Breast Cancer

Anders, C. K., Winer, E. P., Ford, J. M., Dent, R. A., Silver, D. P., Sledge, G. W., & Carey, L. (2010) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-10-0939 · Cited by 154 · see citing works

The flavonoids apigenin and luteolin suppress ultraviolet A-induced matrix metalloproteinase-1 expression via MAPKs and AP-1-dependent signaling in HaCaT cells

Hwang, Y. P., Oh, K. N., Yun, H. J., & Jeong, H. G. (2010) · Journal of Dermatological Science · doi:10.1016/j.jdermsci.2010.10.016 · Cited by 132 · see citing works

Ultrastructural localization of CD38 immunoreactivity in rat brain

Yamada, M., Mizuguchi, M., Otsuka, N., Ikeda, K., & Takahashi, H. (1997) · Brain Research · doi:10.1016/s0006-8993(97)00117-0 · Cited by 111 · see citing works

Flavonoids as inhibitors of human CD38

Kellenberger, E., Kuhn, I., Schuber, F. J., & Muller‐Steffner, H. (2011) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2011.05.022 · Cited by 104 · see citing works

Apigenin Induces Apoptosis in Human Leukemia Cells and Exhibits Anti-Leukemic Activity In Vivo

Budhraja, A., Gao, N., Zhang, Z., Son, Y., Cheng, S., Wang, X., Ding, S., Hitron, J. A., Chen, G., Luo, J., et al. (2011) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-11-0343 · Cited by 103 · see citing works

p53 polymorphism in codon 72 and risk of human papillomavirus-induced cervical cancer: effect of inter-laboratory variation

Makni, H., Franco, E. L., Kaiano, J. H. L., Villa, L. L., Labrecque, S., Dudley, R., Storey, A., & Matlashewski, G. (2000) · International Journal of Cancer · doi:10.1002/1097-0215(20000815)87:4 · Cited by 99 · see citing works

Poly(ADP-ribose) Polymerase-1 Is a Nuclear Epigenetic Regulator of Mitochondrial DNA Repair and Transcription

Lapucci, A., Pittelli, M. G., Rapizzi, E., Felici, R., Moroni, F., & Chiarugi, A. (2011) · Molecular Pharmacology · doi:10.1124/mol.110.070110 · Cited by 65 · see citing works

Apigenin inhibits release of inflammatory mediators by blocking the NF-κB activation pathways in the HMC-1 cells

Kang, O., Lee, J. H., & Kwon, D. (2010) · Immunopharmacology and Immunotoxicology · doi:10.3109/08923973.2010.538851 · Cited by 60 · see citing works

Synthesis of NAADP and cADPR in Mitochondria

Liang, M., Chini, E. N., Cheng, J., & Dousa, T. P. (1999) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1999.1463 · Cited by 53 · see citing works

Executive summary of the Strategic Plan for National Institutes of Health Obesity Research

Spiegel, A. M., & Alving, B. M. (2005) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/82.1.221s · Cited by 41 · see citing works

Apigenin inhibits tumor necrosis factor α–induced cell proliferation and prostaglandin E2 synthesis by inactivating NFκB in endometriotic stromal cells

Suou, K., Taniguchi, F., Tagashira, Y., Kiyama, T., Terakawa, N., & Harada, T. (2010) · Fertility and Sterility · doi:10.1016/j.fertnstert.2010.09.046 · Cited by 31 · see citing works

Executive summary of the Strategic Plan for National Institutes of Health Obesity Research

Spiegel, A. M., & Alving, B. M. (2005) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/82.1.211s · Cited by 23 · see citing works

NAD+ Metabolism and the Control of Energy Homeostasis: A Balancing Act between Mitochondria and the Nucleus

Cantó, C., Menzies, K. J., & Auwerx, J. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.05.023 · Cited by 1,648 · see citing works

NAD+ metabolism and its roles in cellular processes during ageing

Covarrubias, A. J., Perrone, R., Grozio, A., & Verdin, E. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-00313-x · Cited by 1,617 · see citing works

NAD+ and sirtuins in aging and disease

Imai, S.-I., & Guarente, L. (2014) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.04.002 · Cited by 1,481 · see citing works

CD38 Dictates Age-Related NAD Decline and Mitochondrial Dysfunction through an SIRT3-Dependent Mechanism

Camacho-Pereira, J., Tarragó, M. G., Chini, C. C. S., Nin, V., Escande, C., Warner, G. M., Puranik, A. S., Schoon, R. A., Reid, J. M., Galina, A., et al. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.05.006 · Cited by 901 · see citing works

Therapeutic Potential of NAD-Boosting Molecules: The In Vivo Evidence

Rajman, L., Chwalek, K., & Sinclair, D. A. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.02.011 · Cited by 865 · see citing works

Slowing ageing by design: the rise of NAD+ and sirtuin-activating compounds

Bonkowski, M. S., & Sinclair, D. A. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.93 · Cited by 834 · see citing works

How the Warburg effect supports aggressiveness and drug resistance of cancer cells?

Icard, P., Shulman, S. D., Farhat, D., Steyaert, J., Alifano, M., & Lincet, H. (2018) · Drug Resistance Updates · doi:10.1016/j.drup.2018.03.001 · Cited by 648 · see citing works

NAD+ homeostasis in health and disease

Katsyuba, E., Romani, M., Hofer, D., & Auwerx, J. (2020) · Nature Metabolism · doi:10.1038/s42255-019-0161-5 · Cited by 627 · see citing works

Interventions to slow aging in humans: are we ready?

Longo, V. D., Antebi, A., Bartke, A., Barzilai, N., Brown‐Borg, H. M., Caruso, C., Curiel, T. J., Cabo, R., Franceschi, C., Gems, D., et al. (2015) · Aging Cell · doi:10.1111/acel.12338 · Cited by 592 · see citing works

NAD(+) in aging: molecular mechanisms and translational implications

Fang, E. F., Lautrup, S., Hou, Y., Demarest, T. G., Croteau, D. L., Mattson, M. P., & Bohr, V. A. (2017) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2017.08.001 · Cited by 501 · see citing works

Sirtuins and NAD + in the Development and Treatment of Metabolic and Cardiovascular Diseases

Kane, A. E., & Sinclair, D. A. (2018) · Circulation Research · doi:10.1161/circresaha.118.312498 · Cited by 490 · see citing works

Sirtuins, a promising target in slowing down the ageing process

Grabowska, W., Sikora, E., & Bielak-Zmijewska, A. (2017) · Biogerontology · doi:10.1007/s10522-017-9685-9 · Cited by 470 · see citing works

It takes two to tango: NAD(+) and sirtuins in aging/longevity control

Imai, S.-I., & Guarente, L. (2016) · npj Aging and Mechanisms of Disease · doi:10.1038/npjamd.2016.17 · Cited by 394 · see citing works

A Potent and Specific CD38 Inhibitor Ameliorates Age-Related Metabolic Dysfunction by Reversing Tissue NAD+ Decline

Tarragó, M. G., Chini, C. C. S., Kanamori, K. S., Warner, G. M., Caride, A., de Oliveira, G. C., Rud, M., Samani, A., Hein, K. Z., Huang, R., et al. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.03.016 · Cited by 384 · see citing works

Quercetin and metabolic syndrome: A review

Hosseini, A., Razavi, B. M., Banach, M., & Hosseinzadeh, H. (2021) · Phytotherapy Research · doi:10.1002/ptr.7144 · Cited by 390 · see citing works

Role of NAD+ in regulating cellular and metabolic signaling pathways

Amjad, S., Nisar, S., Bhat, A. A., Shah, A. R., Frenneaux, M. P., Fakhro, K. A., Haris, M., Reddy, R. D., Patay, Z. J., Baur, J. A., et al. (2021) · Molecular Metabolism · doi:10.1016/j.molmet.2021.101195 · Cited by 394 · see citing works

The Multi-faceted Ecto-enzyme CD38: Roles in Immunomodulation, Cancer, Aging, and Metabolic Diseases

Hogan, K. A., Chini, C. C. S., & Chini, E. N. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.01187 · Cited by 337 · see citing works

Repairing mitochondrial dysfunction in disease

Sorrentino, V., Menzies, K. J., & Auwerx, J. (2018) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010716-104908 · Cited by 337 · see citing works

CD38: An Immunomodulatory Molecule in Inflammation and Autoimmunity

Piedra-Quintero, Z. L., Wilson, Z., Nava, P., & Guerau‐de‐Arellano, M. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.597959 · Cited by 339 · see citing works

Protein acetylation in metabolism – metabolites and cofactors

Menzies, K. J., Zhang, H., Katsyuba, E., & Auwerx, J. (2016) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2015.181 · Cited by 331 · see citing works

Quercetin reduces obesity-associated ATM infiltration and inflammation in mice: a mechanism including AMPKα1/SIRT1

Dong, J., Zhang, X., Zhang, L., Bian, H., Xu, N., Bao, B., & Liu, J. (2014) · Journal of Lipid Research · doi:10.1194/jlr.m038786 · Cited by 295 · see citing works

Kynurenine pathway, NAD+ synthesis, and mitochondrial function: Targeting tryptophan metabolism to promote longevity and healthspan

Castro-Portuguez, R., & Sutphin, G. L. (2020) · Experimental Gerontology · doi:10.1016/j.exger.2020.110841 · Cited by 282 · see citing works

Pharmacokinetic properties and drug interactions of apigenin, a natural flavone

Tang, D., Chen, K., Huang, L., & Li, J. (2016) · Expert Opinion on Drug Metabolism & Toxicology · doi:10.1080/17425255.2017.1251903 · Cited by 249 · see citing works

Mitochondria: Their relevance during oocyte ageing

van der Reest, J., Cecchino, G. N., Haigis, M. C., & Kordowitzki, P. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101378 · Cited by 253 · see citing works

NAD+ homeostasis in human health and disease

Perez, R. Z., Wanders, R. J. A., van Karnebeek, C., & Houtkooper, R. H. (2021) · EMBO Molecular Medicine · doi:10.15252/emmm.202113943 · Cited by 238 · see citing works

The importance of NAMPT / NAD / SIRT1 in the systemic regulation of metabolism and ageing

Imai, S., & Yoshino, J. (2013) · Diabetes Obesity and Metabolism · doi:10.1111/dom.12171 · Cited by 232 · see citing works

The Pharmacology of CD38/NADase: An Emerging Target in Cancer and Diseases of Aging

Chini, E. N., Chini, C. C. S., Espindola Netto, J. M., de Oliveira, G. C., & van Schooten, W. (2018) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2018.02.001 · Cited by 227 · see citing works

Modulating NAD+ metabolism, from bench to bedside

Katsyuba, E., & Auwerx, J. H. (2017) · The EMBO Journal · doi:10.15252/embj.201797135 · Cited by 224 · see citing works

Nicotinamide Riboside—The Current State of Research and Therapeutic Uses

Mehmel, M., Jovanović, N. D., & Spitz, U. P. (2020) · Nutrients · doi:10.3390/nu12061616 · Cited by 225 · see citing works

NAD and the aging process: role in life, death and everything in between

Chini, C. C. S., Tarragó, M. G., & Chini, E. N. (2017) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2016.11.003 · Cited by 208 · see citing works

Epigenome-wide study identifies novel methylation loci associated with body mass index and waist circumference

Aslibekyan, S. W., Demerath, E. W., Mendelson, M., Zhi, D., Guan, W., Liang, L., Sha, J., Pankow, J. S., Liu, C., Irvin, M. R., et al. (2015) · Obesity · doi:10.1002/oby.21111 · Cited by 210 · see citing works

CD38 Is Robustly Induced in Human Macrophages and Monocytes in Inflammatory Conditions

Amici, S. A., Young, N. A., Miranda, J. N., Jablonski, K., Arcos, J., Rosas, L. E., Papenfuss, T. L., Torrelles, J. B., Jarjour, W. N., & Guerau‐de‐Arellano, M. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.01593 · Cited by 203 · see citing works

The Plasma NAD + Metabolome Is Dysregulated in “Normal” Aging

Clement, J., Wong, M. W. K., Poljak, A., Sachdev, P. S., & Braidy, N. (2018) · Rejuvenation Research · doi:10.1089/rej.2018.2077 · Cited by 196 · see citing works

Senescence-induced inflammation: an important player and key therapeutic target in atherosclerosis

Stojanović, S. D., Fiedler, J., Bauersachs, J., Thum, T., & Sedding, D. G. (2020) · European Heart Journal · doi:10.1093/eurheartj/ehz919 · Cited by 188 · see citing works

Functionality of apigenin as a potent antioxidant with emphasis on bioavailability, metabolism, action mechanism and in vitro and in vivo studies: A review

Kashyap, P., Shikha, D., Thakur, M., & Aneja, A. (2021) · Journal of Food Biochemistry · doi:10.1111/jfbc.13950 · Cited by 182 · see citing works

NAD+ biosynthesis, aging, and disease

Johnson, S., & Imai, S. (2018) · F1000Research · doi:10.12688/f1000research.12120.1 · Cited by 178 · see citing works

Activation of PPARγ by a Natural Flavonoid Modulator, Apigenin Ameliorates Obesity-Related Inflammation Via Regulation of Macrophage Polarization

Feng, X., Weng, D., Zhou, F., Owen, Y. D., Qin, H., Zhao, J., Wenyu, Huang, Y., Chen, J., Fu, H., et al. (2016) · EBioMedicine · doi:10.1016/j.ebiom.2016.06.017 · Cited by 183 · see citing works

Nicotinamide Mononucleotide: A Promising Molecule for Therapy of Diverse Diseases by Targeting NAD+ Metabolism

Hong, W., Mo, F., Zhang, Z., Huang, M., & Wei, X. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00246 · Cited by 179 · see citing works

Sirtuins and their Biological Relevance in Aging and Age-Related Diseases

Zhao, L., Cao, J., Hu, K., He, X., Dou, Y., Tong, T., & Han, L. (2020) · Aging and Disease · doi:10.14336/ad.2019.0820 · Cited by 174 · see citing works

Apigenin Ameliorates Dyslipidemia, Hepatic Steatosis and Insulin Resistance by Modulating Metabolic and Transcriptional Profiles in the Liver of High-Fat Diet-Induced Obese Mice

Jung, U. J., Cho, Y.-Y., & Choi, M. (2016) · Nutrients · doi:10.3390/nu8050305 · Cited by 160 · see citing works

The role of NAD+ metabolism and its modulation of mitochondria in aging and disease

Yusri, K., Jose, S., Vermeulen, K. S., Tan, T. C. M., & Sorrentino, V. (2025) · npj Metabolic Health and Disease · doi:10.1038/s44324-025-00067-0 · Cited by 171 · see citing works

Polyphenolic Phytochemicals in Cancer Prevention and Therapy: Bioavailability versus Bioefficacy

Estrela, J. M., Mena, S., Obrador, E., Benlloch, M., Castellano, G., Palmer, R. S., & Dellinger, R. W. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b01026 · Cited by 144 · see citing works

Anti-inflammatory phytochemicals for the treatment of diabetes and its complications: Lessons learned and future promise

Kong, M., Xie, K., Lv, M., Li, J., Yao, J., Yan, K., Wu, X., Xu, Y., & Ye, D. (2020) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2020.110975 · Cited by 143 · see citing works

Apigenin: A current review on its beneficial biological activities

Zhou, X., Wang, F., Zhou, R., Song, X., & Xie, M.-L. (2017) · Journal of Food Biochemistry · doi:10.1111/jfbc.12376 · Cited by 139 · see citing works

Roles of CD38 in the Immune Response to Infection

Glaría, E., & Valledor, A. F. (2020) · Cells · doi:10.3390/cells9010228 · Cited by 139 · see citing works

NAD metabolism: Role in senescence regulation and aging

Chini, C. C. S., Cordeiro, H. S., Tran, N. L. K., & Chini, E. N. (2023) · Aging Cell · doi:10.1111/acel.13920 · Cited by 138 · see citing works

Location, Location, Location: Compartmentalization of NAD+ Synthesis and Functions in Mammalian Cells

Cambronne, X. A., & Kraus, W. L. (2020) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2020.05.010 · Cited by 137 · see citing works

Why NAD + Declines during Aging: It’s Destroyed

Schultz, M. B., & Sinclair, D. A. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.05.022 · Cited by 126 · see citing works

Niacin

Kirkland, J. B., & Meyer‐Ficca, M. L. (2018) · Advances in food and nutrition research · doi:10.1016/bs.afnr.2017.11.003 · Cited by 134 · see citing works

PEGylated graphene oxide-mediated quercetin-modified collagen hybrid scaffold for enhancement of MSCs differentiation potential and diabetic wound healing

Chu, J., Shi, P., Yan, W., Fu, J., Yang, Z., He, C., Deng, X., & Liu, H. (2018) · Nanoscale · doi:10.1039/c8nr02538j · Cited by 131 · see citing works

CD38 inhibition by apigenin ameliorates mitochondrial oxidative stress through restoration of the intracellular NAD+/NADH ratio and Sirt3 activity in renal tubular cells in diabetic rats

Ogura, Y., Kitada, M., Xu, J., Monno, I., & Koya, D. (2020) · Aging · doi:10.18632/aging.103410 · Cited by 118 · see citing works

Key Signaling Pathways in Aging and Potential Interventions for Healthy Aging

Yu, M., Zhang, H., Wang, B. Z., Zhang, Y., Zheng, X., Shao, B., Zhuge, Q., & Jin, K. (2021) · Cells · doi:10.3390/cells10030660 · Cited by 114 · see citing works

Potential Modulation of Sirtuins by Oxidative Stress

Santos, L., Escande, C., & Denicola, A. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/9831825 · Cited by 115 · see citing works

Therapeutic application of natural products: NAD+ metabolism as potential target

Guo, C., Huang, Q., Wang, Y., Yao, Y., Li, J., Chen, J., Wu, M., Zhang, Z., Mingyao, E., Qi, H., et al. (2023) · Phytomedicine · doi:10.1016/j.phymed.2023.154768 · Cited by 114 · see citing works

Interplay between compartmentalized NAD + synthesis and consumption: a focus on the PARP familyPreprint

Cohen, M. S. (2020) · Genes & Development · doi:10.1101/gad.335109.119 · Cited by 109 · see citing works

Apigenin ameliorates HFD-induced NAFLD through regulation of the XO/NLRP3 pathways

Lv, Y., Gao, X., Luo, Y., Fan, W., Shen, T., Ding, C., Yao, M., Song, S., & Yan, L. (2019) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2019.05.015 · Cited by 108 · see citing works

Dietary plant flavonoids in prevention of obesity and diabetes

Dinda, B., Dinda, M., Roy, A., & Dinda, S. (2019) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2019.08.006 · Cited by 106 · see citing works

Electrically Triggered Drug Delivery from Novel Electrospun Poly(Lactic Acid)/Graphene Oxide/Quercetin Fibrous Scaffolds for Wound Dressing Applications

Croitoru, A.-M., Karaçelebi, Y., Saatcioglu, E., Altan, E., Ulağ, S., Aydoğan, H. K., Şahin, A., Motelică, L., Oprea, O., Tihăuan, B.-M., et al. (2021) · Pharmaceutics · doi:10.3390/pharmaceutics13070957 · Cited by 104 · see citing works

Differential effects of dietary flavonoids on adipogenesis

Khalilpourfarshbafi, M., Gholami, K., Murugan, D. D., Sattar, M. Z. A., & Abdullah, N. A. (2018) · European Journal of Nutrition · doi:10.1007/s00394-018-1663-8 · Cited by 106 · see citing works

Rutin increases muscle mitochondrial biogenesis with AMPK activation in high-fat diet-induced obese rats.

Seo, S., Lee, M.-S., Chang, E., Shin, Y., Oh, S., Kim, I.-H., & Kim, Y. (2015) · Nutrients · doi:10.3390/nu7095385 · Cited by 100 · see citing works

Blockade of CD38 diminishes lipopolysaccharide-induced macrophage classical activation and acute kidney injury involving NF-κB signaling suppression

Shu, B., Ye, F., Gui, Y., Lu, Q., Wei, W., Xue, X., Sun, X., He, W., Yang, J., & Dai, C. (2017) · Cellular Signalling · doi:10.1016/j.cellsig.2017.10.014 · Cited by 100 · see citing works

Mitochondria Are Dynamically Transferring Between Human Neural Cells and Alexander Disease-Associated GFAP Mutations Impair the Astrocytic Transfer

Gao, L., Zhang, Z., Lü, J., & Pei, G. (2019) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2019.00316 · Cited by 98 · see citing works

Accurate Measurement of Nicotinamide Adenine Dinucleotide (NAD+) with High-Performance Liquid Chromatography

Yoshino, J., & Imai, S. (2013) · Methods in molecular biology · doi:10.1007/978-1-62703-637-5_14 · Cited by 95 · see citing works

Roles of Mitochondrial Sirtuins in Mitochondrial Function, Redox Homeostasis, Insulin Resistance and Type 2 Diabetes

Wang, C., & Wei, Y. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21155266 · Cited by 95 · see citing works

Targeting NAD+ in Metabolic Disease: New Insights Into an Old Molecule

Elhassan, Y., Philp, A., & Lavery, G. G. (2017) · Journal of the Endocrine Society · doi:10.1210/js.2017-00092 · Cited by 92 · see citing works

Sirtuins as Important Factors in Pathological States and the Role of Their Molecular Activity Modulators

Kratz, E. M., Sołkiewicz, K., Kubis-Kubiak, A., & Piwowar, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22020630 · Cited by 93 · see citing works

Inhibition of CD38 and supplementation of nicotinamide riboside ameliorate lipopolysaccharide‐induced microglial and astrocytic neuroinflammation by increasing NAD+

Roboon, J., Hattori, T., Ishii, H., Takarada‐Iemata, M., Nguyen, D. T., Heer, C. D., O’Meally, D., Brenner, C., Yamamoto, Y., Okamoto, H., et al. (2021) · Journal of Neurochemistry · doi:10.1111/jnc.15367 · Cited by 93 · see citing works

Apigenin prevents metabolic syndrome in high-fructose diet-fed mice by Keap1-Nrf2 pathway

Yang, M. H., Jiang, Z., Li, C.-G., Zhu, Y., Li, Z., Tang, Y., & Ni, C. (2018) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2018.06.108 · Cited by 88 · see citing works

The CD38 glycohydrolase and the NAD sink: implications for pathological conditions

Zeidler, J. D., Hogan, K. A., Agorrody, G., Peclat, T., Kashyap, S., Kanamori, K. S., Gomez, L. S., Mazdeh, D. Z., Warner, G. M., Thompson, K. L., et al. (2022) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00451.2021 · Cited by 90 · see citing works

NAMPT as a Therapeutic Target against Stroke

Wang, P., & Miao, C. (2015) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2015.08.012 · Cited by 86 · see citing works

Therapeutic potential of boosting NAD+ in aging and age-related diseases

Aman, Y., Qiu, Y., Tao, J., & Fang, E. F. (2018) · Translational Medicine of Aging · doi:10.1016/j.tma.2018.08.003 · Cited by 85 · see citing works

Apigenin Ameliorates the Obesity-Induced Skeletal Muscle Atrophy by Attenuating Mitochondrial Dysfunction in the Muscle of Obese Mice

Choi, W. H., Son, H. J., Jang, Y. J., Ahn, J., Jung, C. H., & Ha, T. Y. (2017) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201700218 · Cited by 81 · see citing works

Aryl hydrocarbon receptor (AHR) functions: Balancing opposing processes including inflammatory reactions

Bock, K. W. (2020) · Biochemical Pharmacology · doi:10.1016/j.bcp.2020.114093 · Cited by 81 · see citing works

Nicotinamide adenine dinucleotide: Biosynthesis, consumption and therapeutic role in cardiac diseases

Tannous, C., Booz, G. W., Altara, R., Muhieddine, D. H., Mericskay, M., Refaat, M. M., & Zouein, F. A. (2020) · Acta Physiologica · doi:10.1111/apha.13551 · Cited by 79 · see citing works

Pharmacological Properties of 4′, 5, 7-Trihydroxyflavone (Apigenin) and Its Impact on Cell Signaling Pathways

Abid, R., Ghazanfar, S., Farid, A., Sulaman, S. M., Idrees, M., Amen, R. A., Muzammal, M., Shahzad, M. K., Mohamed, M. O., Khaled, A. A., et al. (2022) · Molecules · doi:10.3390/molecules27134304 · Cited by 79 · see citing works

Antiaging effects of bioactive molecules isolated from plants and fungi

Martel, J., Ojcius, D. M., Ko, Y., Chang, C., & Young, J. D. (2019) · Medicinal Research Reviews · doi:10.1002/med.21559 · Cited by 79 · see citing works

Roles of Pyruvate, NADH, and Mitochondrial Complex I in Redox Balance and Imbalance inβCell Function and Dysfunction

Luo, X., Li, R., & Yan, L. (2015) · Journal of Diabetes Research · doi:10.1155/2015/512618 · Cited by 77 · see citing works

Nicotinamide Adenine Dinucleotide Metabolism and Neurodegeneration

Pehar, M., Harlan, B. A., Killoy, K. M., & Vargas, M. R. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7145 · Cited by 77 · see citing works

Troxerutin improves hepatic lipid homeostasis by restoring NAD+-depletion-mediated dysfunction of lipin 1 signaling in high-fat diet-treated mice

Zhang, Z.-F., Fan, S., Zheng, Y., Lu, J. L., Wu, D., Shan, Q., & Hu, B. (2014) · Biochemical Pharmacology · doi:10.1016/j.bcp.2014.07.002 · Cited by 75 · see citing works

Procyanidins and Alzheimer’s Disease

Zhao, S., Zhang, L., Yang, C., Li, Z., & Rong, S. (2019) · Molecular Neurobiology · doi:10.1007/s12035-019-1469-6 · Cited by 74 · see citing works

Mitochondrial Hyperacetylation in the Failing Hearts of Obese Patients Mediated Partly by a Reduction in SIRT3: The Involvement of the Mitochondrial Permeability Transition Pore

Castillo, E. C., Morales, J. A., Chapoy‐Villanueva, H., Silva‐Platas, C., Treviño‐Saldaña, N., Guerrero-Beltrán, C. E., Bernal‐Ramírez, J., Torres‐Quintanilla, A., García, N., Youker, K. A., et al. (2019) · Cellular Physiology and Biochemistry · doi:10.33594/000000151 · Cited by 74 · see citing works

At the interface of antioxidant signalling and cellular function: Key polyphenol effects

Kerimi, A., & Williamson, G. (2016) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201500940 · Cited by 71 · see citing works

Regulation of NAD biosynthetic enzymes modulates NAD-sensing processes to shape mammalian cell physiology under varying biological cues

Ruggieri, S., Orsomando, G., Sorci, L., & Raffaelli, N. (2015) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2015.02.021 · Cited by 71 · see citing works

Keeping the balance in NAD metabolism

Strømland, Ø., Niere, M., Nikiforov, A. A., VanLinden, M. R., Heiland, I., & Ziegler, M. (2019) · Biochemical Society Transactions · doi:10.1042/bst20180417 · Cited by 72 · see citing works

The flavonoid compound apigenin prevents colonic inflammation and motor dysfunctions associated with high fat diet-induced obesity

Gentile, D., Fornai, M., Colucci, R., Pellegrini, C., Tirotta, E., Benvenuti, L., Segnani, C., Ippolito, C., Duranti, E., Virdis, A., et al. (2018) · PLoS ONE · doi:10.1371/journal.pone.0195502 · Cited by 71 · see citing works

Interplay between NADH oxidation by complex I, glutathione redox state and sirtuin-3, and its role in the development of insulin resistance

Cortés‐Rojo, C., Vargas-Vargas, M. A., Olmos‐Orizaba, B. E., Rodríguez-Orozco, A. R., & Calderón‐Cortés, E. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2020.165801 · Cited by 70 · see citing works

Aryl hydrocarbon receptor (AHR)-mediated inflammation and resolution: Non-genomic and genomic signaling

Bock, K. W. (2020) · Biochemical Pharmacology · doi:10.1016/j.bcp.2020.114220 · Cited by 70 · see citing works

Luteolinidin Protects the Postischemic Heart through CD38 Inhibition with Preservation of NAD(P)(H)

Boslett, J., Hemann, C., Zhao, Y. J., Lee, H.-C., & Zweier, J. L. (2017) · The Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.116.239459 · Cited by 69 · see citing works

Troxerutin protects against 2,2′,4,4′-tetrabromodiphenyl ether (BDE-47)-induced liver inflammation by attenuating oxidative stress-mediated NAD+-depletion

Zhang, Z.-F., Zhang, Y., Fan, S., Zhuang, J., Zheng, Y., Lu, J. L., Wu, D., Shan, Q., & Hu, B. (2014) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2014.09.012 · Cited by 68 · see citing works

Discovery of small-molecule activators of nicotinamide phosphoribosyltransferase (NAMPT) and their preclinical neuroprotective activity

Hong, Y., Liu, M., Wang, L., Zu, Y., Wu, C., Li, C., Zhang, R., Lu, H., Li, F., Xi, S., et al. (2022) · Cell Research · doi:10.1038/s41422-022-00651-9 · Cited by 69 · see citing works

Differential Impact of Flavonoids on Redox Modulation, Bioenergetics, and Cell Signaling in Normal and Tumor Cells: A Comprehensive Review

Kerimi, A., & Williamson, G. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7086 · Cited by 66 · see citing works

Nutraceutical Activation of Sirt1: A Review

DiNicolantonio, J. J., McCarty, M. F., & O'Keefe, J. H. (2022) · Open Heart · doi:10.1136/openhrt-2022-002171 · Cited by 65 · see citing works

NAD-Biosynthetic and Consuming Enzymes as Central Players of Metabolic Regulation of Innate and Adaptive Immune Responses in Cancer

Audrito, V., Managò, A., Gaudino, F., Sorci, L., Messana, V. G., Raffaelli, N., & Deaglio, S. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.01720 · Cited by 64 · see citing works

Cellular Compartmentation and the Redox/Nonredox Functions of NAD +

Kulkarni, C. A., & Brookes, P. S. (2019) · Antioxidants and Redox Signaling · doi:10.1089/ars.2018.7722 · Cited by 64 · see citing works

Structurally Different Flavonoid Subclasses Attenuate High-Fat and High-Fructose Diet Induced Metabolic Syndrome in Rats

Zhang, J., Zhao, L., Cheng, Q., Ji, B., Yang, M., Sanidad, K. Z., Wang, C., & Zhou, F. L. (2018) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.8b03574 · Cited by 63 · see citing works

Beneficial effects of celery ( Apium graveolens ) on metabolic syndrome: A review of the existing evidences

Hedayati, N., Naeini, M. B., Mohammadinejad, A., & Mohajeri, S. A. (2019) · Phytotherapy Research · doi:10.1002/ptr.6492 · Cited by 63 · see citing works

Human geroprotector discovery by targeting the converging subnetworks of aging and age-related diseases

Yang, J., Peng, S., Zhang, B., Houten, S. M., Schadt, E. E., Zhu, J., Suh, Y., & Tu, Z. (2019) · GeroScience · doi:10.1007/s11357-019-00106-x · Cited by 64 · see citing works

The balance between NAD+ biosynthesis and consumption in ageing

Strømland, Ø., Diab, J., Ferrario, E., Sverkeli, L. J., & Ziegler, M. (2021) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2021.111569 · Cited by 63 · see citing works

Flavonoid Apigenin Is an Inhibitor of the NAD+ase CD38 Implications for Cellular NAD+ Metabolism, Protein Acetylation, and Treatment of Metabolic Syndrome

(2016)

The CD38 Inhibitor, Apigenin, Ameliorates Obesity-Related Metabolic and Inflammatory Dysfunction via Boosting the NAD+/SIRT1 Axis in Rats on High Fat Diet

Rezk, B. T., Habib, M. Z., El-kholy, N. M., Mohamad, M. I., Adel, S., Hassan, M. N. M., Sadek, D. R., & Elayat, W. M. (2026) · Journal of Evolutionary Biochemistry and Physiology · doi:10.1134/s0022093025600630

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 · see citing works

CD38 as a Regulator of Cellular NAD: A Novel Potential Pharmacological Target for Metabolic Conditions

Chini, E. N. (2009) · Current Pharmaceutical Design · doi:10.2174/138161209787185788 · Cited by 193 · see citing works

The importance of pharmacological modulation of the enzymatic activity of CD38 and intracellular NAD levels

Al-Abady, Z. N., Jabbar, N. K., & Alfarhani, B. F. (2019) · Journal of Physics Conference Series · doi:10.1088/1742-6596/1294/5/052073