Inhibition of CD38 with the Thiazoloquin(az)olin(on)e 78c Protects the Heart against Postischemic Injury
Open accessAbstract
Inhibition of and genetic deletion of the NAD(P)+ hydrolase [NAD(P)ase] CD38 have been shown to protect against ischemia/reperfusion (I/R) injury in rat and mouse hearts. CD38 has been shown to enhance salvage of NADP(H), which in turn prevents impairment of endothelial nitric oxide synthase function, a hallmark of endothelial dysfunction. Despite growing evidence for a role of CD38 in postischemic injury, until recently there had been a lack of potent CD38 inhibitors. Recently, a new class of thiazoloquin(az)olin(on)e compounds were identified as highly potent and specific CD38 inhibitors. Herein, we investigate the ability of one of these compounds, 78c, to inhibit CD38 and protect the heart in an ex vivo model of myocardial I/R injury. The potency and mechanism of CD38 inhibition by 78c was assessed in vitro using recombinant CD38. The dose-dependent tissue uptake of 78c in isolated mouse hearts was determined, and high tissue permeability of 78c was observed when delivered in perfusate. Treatment of hearts with 78c was protective against both postischemic endothelial and cardiac myocyte injury, with preserved nitric oxide synthase-dependent vasodilatory and contractile function, respectively. Myocardial infarction was also significantly decreased in 78c-treated hearts, with preserved levels of high-energy phosphates. Protective effects peaked at 10 μ M treatment, and similar protection without toxicity was seen at 5-fold higher doses. Overall, 78c was shown to be a potent and biologically active CD38 inhibitor with favorable tissue uptake and marked protective effects against I/R injury with enhanced preservation of contractile function, coronary flow, and decreased infarction.
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
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?
Treating aged mice with compound 78c improves muscle function.
“78c also prevents age-related declines in NAD+ levels in mice, and treatment of aged mice with this compound was shown to ameliorate metabolic dysfunction, reduce DNA damage accumulation and improve muscle function91,231.”
From NAD+ metabolism and its roles in cellular processes during ageing (2021) · cites this paper as [231]
Treating aged mice with compound 78c reduces DNA damage accumulation.
“78c also prevents age-related declines in NAD+ levels in mice, and treatment of aged mice with this compound was shown to ameliorate metabolic dysfunction, reduce DNA damage accumulation and improve muscle function91,231.”
From NAD+ metabolism and its roles in cellular processes during ageing (2021) · cites this paper as [231]
Compound 78c prevents age-related NAD+ decline in mice.
“78c also prevents age-related declines in NAD+ levels in mice, and treatment of aged mice with this compound was shown to ameliorate metabolic dysfunction, reduce DNA damage accumulation and improve muscle function91,231.”
From NAD+ metabolism and its roles in cellular processes during ageing (2021) · cites this paper as [231]
Treating aged mice with compound 78c lessens metabolic dysfunction.
“78c also prevents age-related declines in NAD+ levels in mice, and treatment of aged mice with this compound was shown to ameliorate metabolic dysfunction, reduce DNA damage accumulation and improve muscle function91,231.”
From NAD+ metabolism and its roles in cellular processes during ageing (2021) · cites this paper as [231]
Compound 78c protects against endothelial and cardiac muscle cell injury after ischaemia in mice.
“More recently, compound 78c protected against postischaemic endothelial and cardiac myocyte injury in mice91,231.”
From NAD+ metabolism and its roles in cellular processes during ageing (2021) · cites this paper as [231]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
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
Evolution and function of the ADP ribosyl cyclase/CD38 gene family in physiology and pathology
Malavasi, F., Deaglio, S., Funaro, A., Ferrero, E., Horenstein, A. L., Ortolan, E., Vaisitti, T., & Aydin, S. (2008) · Physiological Reviews · doi:10.1152/physrev.00035.2007 · Cited by 862 · see citing works
CD38 is critical for social behaviour by regulating oxytocin secretion
Jin, D., Liu, H.-X., Hirai, H., Torashima, T., Nagai, T., Lopatina, O., Shnayder, N. A., Yamada, K., Noda, M., Seike, T., et al. (2007) · Nature · doi:10.1038/nature05526 · Cited by 665 · see citing works
Neely, J. R., & Grotyohann, L. W. (1984) · Circulation Research · doi:10.1161/01.res.55.6.816 · Cited by 579 · see citing works
Zimmerman, A. N. E., & Hülsmann, W. C. (1966) · Nature · doi:10.1038/211646a0 · Cited by 479 · see citing works
CD38 expression as an important prognostic factor in B-cell chronic lymphocytic leukemia
Ibrahim, S., Keating, M. J., Do, K.-A., O'Brien, S. M., Huh, Y. O., Jilani, I. B., Lerner, S. A., Kantarjian, H. M., & Albitar, M. X. (2001) · Blood · doi:10.1182/blood.v98.1.181 · Cited by 451 · see citing works
Partida-Sánchez, S., Cockayne, D. A., Monard, S., Jacobson, E. L., Oppenheimer, N., Garvy, B., Kusser, K., Goodrich, S., Howard, M., Harmsen, A., et al. (2001) · Nature Medicine · doi:10.1038/nm1101-1209 · Cited by 450 · see citing works
Bailey, S., & Ayling, J. E. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0902072106 · Cited by 421 · see citing works
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
Self-citationRegulation 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
Properties of 3-Deoxyanthocyanins from Sorghum
Awika, J. M., Rooney, L. W., & Waniska, R. D. (2004) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf049653f · Cited by 327 · see citing works
Calcium-mediated cell death during myocardial reperfusion
García‐Dorado, D., Ruiz‐Meana, M., Inserte, J., Rodríguez‐Sinovas, A., & Piper, H. M. (2012) · Cardiovascular Research · doi:10.1093/cvr/cvs116 · Cited by 308 · see citing works
CD38 and CD157: A long journey from activation markers to multifunctional molecules
Quarona, V., Zaccarello, G., Chillemi, A., Brunetti, E., Singh, V. K., Ferrero, E., Funaro, A., Horenstein, A. L., & Malavasi, F. (2013) · Cytometry Part B Clinical Cytometry · doi:10.1002/cyto.b.21092 · Cited by 269 · see citing works
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
Cockayne, D. A., Muchamuel, T., Grimaldi, J. C., Muller‐Steffner, H., Randall, T. D., Lund, F. E., Murray, R., Schuber, F. J., & Howard, M. (1998) · Blood · doi:10.1182/blood.v92.4.1324 · Cited by 219 · see citing works
Kato, I., Yamamoto, Y., Fujimura, M., Noguchi, N., Takasawa, S., & Okamoto, H. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.4.1869 · Cited by 211 · see citing works
Chini, E. N. (2009) · Current Pharmaceutical Design · doi:10.2174/138161209787185788 · Cited by 193 · see citing works
Imahashi, K., Schneider, M. D., Steenbergen, C., & Murphy, E. (2004) · Circulation Research · doi:10.1161/01.res.0000143898.67182.4c · Cited by 193 · see citing works
Dumitrescu, C., Biondi, R., Xia, Y., Cardounel, A. J., Druhan, L. J., Ambrosio, G., & Zweier, J. L. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0702986104 · Cited by 192 · see citing works
Self-citationKlaidman, L. K., Leung, A. C., & Adams, J. D., Jr. (1995) · Analytical Biochemistry · doi:10.1006/abio.1995.1356 · Cited by 147 · see citing works
Haffner, C. D., Becherer, J. D., Boros, E. E., Cadilla, R., Carpenter, T., Cowan, D., Deaton, D. N., Guo, Y., Harrington, W., Henke, B. R., et al. (2015) · Journal of Medicinal Chemistry · doi:10.1021/jm502009h · Cited by 137 · see citing works
De Pascali, F., Hemann, C., Samons, K., Chen, C.-A., & Zweier, J. L. (2014) · Biochemistry · doi:10.1021/bi500076r · Cited by 131 · see citing works
Self-citationDeshpande, D. A., White, T. A., Doğan, S., Walseth, T. F., Panettieri, R. A., & Kannan, M. (2005) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00217.2004 · Cited by 114 · see citing works
Human CD38 is an authentic NAD(P)+ glycohydrolase
Berthelier, V., Tixier, J. M., Muller‐Steffner, H., Schuber, F. J., & Déterre, P. (1998) · Biochemical Journal · doi:10.1042/bj3301383 · Cited by 109 · 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
Graeff, R. M., Liu, Q., Kriksunov, I. A., Hao, Q., & Lee, H. C. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m604370200 · Cited by 97 · see citing works
Chini, E. N., Chini, C. C. S., Kato, I., Takasawa, S., & OKAMOTO, H. (2002) · Biochemical Journal · doi:10.1042/0264-6021:3620125 · Cited by 96 · see citing works
Guan, X., Liu, X., Hong, X., Zhao, N., Xiao, Y., Wang, L.-F., Tang, L., Jiang, K., Qian, Y., Deng, K., et al. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/7410257 · Cited by 90 · see citing works
Choe, C., Lardong, K., Gelderblom, M., Ludewig, P., Leypoldt, F., Koch‐Nolte, F., Gerloff, C. P., & Magnus, T. U. (2011) · PLoS ONE · doi:10.1371/journal.pone.0019046 · Cited by 82 · see citing works
Inhibition of glioma progression by a newly discovered CD38 inhibitor
Blacher, E., Baruch, B. B., Levy, A., Geva, N., Green, K. D., Garneau‐Tsodikova, S., Fridman, M., & Stein, R. (2014) · International Journal of Cancer · doi:10.1002/ijc.29095 · Cited by 69 · 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
Self-citationReyes, L. A., Boslett, J. J., Varadharaj, S., Pascali, F. D., Hemann, C. F., Druhan, L. J., Ambrosio, G., El‐Mahdy, M. A., & Zweier, J. L. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1505556112 · Cited by 65 · see citing works
Self-citationBoslett, J., Hemann, C., Christofi, F. L., & Zweier, J. L. (2018) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00139.2017 · Cited by 65 · see citing works
Self-citationChini, E. N., Chini, C. C. S., Kato, I., et al. (2002) · Biochemical Journal · doi:10.1042/bj3620125 · Cited by 60 · see citing works
2′-Phospho-Cyclic ADP-ribose, a Calcium-mobilizing Agent Derived from NADP
Vu, C. Q., Lu, P., Chen, C., & Jacobson, M. K. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.9.4747 · Cited by 58 · see citing works
Becherer, J. D., Boros, E. E., Carpenter, T. Y., Cowan, D. J., Deaton, D. N., Haffner, C. D., Jeune, M. R., Kaldor, I. W., Poole, J. C., Preugschat, F., et al. (2015) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b00992 · Cited by 55 · see citing works
Mechanism of Ca2+ overload in endothelial cells exposed to simulated ischemia
Ladilov, Y. V. (2000) · Cardiovascular Research · doi:10.1016/s0008-6363(00)00108-5 · Cited by 45 · see citing works
Boslett, J. J., Helal, M., Chini, E. N., & Zweier, J. L. (2018) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2018.02.015 · Cited by 39 · see citing works
Self-citationHan, M., Kim, S.-J., Park, Y., Shin, Y., Park, H.-J., Park, K.-J., Park, K., Kim, H.-K., Jang, S. I., An, N., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m106439200 · Cited by 38 · see citing works
Design, Synthesis and SAR Studies of NAD Analogues as Potent Inhibitors towards CD38 NADase
Wang, S., Zhu, W., Wang, X., Li, J., Zhang, K., Zhang, L., Zhao, Y. J., Lee, H., & Zhang, L. (2014) · Molecules · doi:10.3390/molecules191015754 · Cited by 32 · see citing works
Sepiapterin Reductase Mediates Chemical Redox Cycling in Lung Epithelial Cells
Yang, S., Jan, Y.-H., Gray, J. P., Mishin, V. M., Heck, D. E., Laskin, D. L., & Laskin, J. D. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.402164 · Cited by 25 · see citing works
CD38 Structure-Based Inhibitor Design Using the N1-Cyclic Inosine 5′-Diphosphate Ribose Template
Moreau, C., Liu, Q., Graeff, R. M., Wagner, G. K., THOMAS, M. P., Swarbrick, J. M., Shuto, S., Lee, H. C., Hao, Q., & Potter, B. V. L. (2013) · PLoS ONE · doi:10.1371/journal.pone.0066247 · Cited by 25 · see citing works
Endothelial dysfunction does not require loss of endothelial nitric oxide synthase
Giraldez, R. R., Panda, A., & Zweier, J. L. (2000) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.2000.278.6.h2020 · Cited by 19 · see citing works
Self-citationGraeff, R. M., & Lee, H. C. (2013) · Methods in molecular biology · doi:10.1007/978-1-62703-441-8_4 · Cited by 9 · see citing works
Choe, C., Lardong, K., Gelderblom, M., Ludewig, P., Leypoldt, F., Koch‐Nolte, F., Gerloff, C. P., & Magnus, T. U. (2011) · PLoS ONE · doi:10.1371/annotation/295c388d-013d-4bb9-b4e4-da8e88317594 · Cited by 7 · see citing works
[The synthesis of purine derivatives and its inhibitory activity on CD38 NADase].
Li, N., Zhu, W., Xue, X.-W., Zhao, Y. J., Lee, H.-C., Zhang, L., & Zhang, L. (2015) · PubMed · Cited by 1 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
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+ 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
NAD + Metabolism in Cardiac Health, Aging, and Disease
Abdellatif, M., Sedej, S., & Kroemer, G. (2021) · Circulation · doi:10.1161/circulationaha.121.056589 · Cited by 262 · see citing works
Targeting CD38-dependent NAD+ metabolism to mitigate multiple organ fibrosis
Shi, B., Wang, W., Korman, B. D., Li, K., Wang, Q., Wei, J., Bale, S., Marangoni, R. G., Bhattacharyya, S., Miller, S. D., et al. (2020) · iScience · doi:10.1016/j.isci.2020.101902 · Cited by 72 · see citing works
Qiu, Y.-M., Xu, S., Chen, X., Wu, X., Zhou, Z., Zhang, J.-N., Tu, Q., Dong, B., Liu, Z.-F., He, J., et al. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01577-3 · Cited by 58 · see citing works
Elmahdy, M., Abdelghany, T. M., Hemann, C. F., Ewees, M. G., Mahgoup, E. M., Eid, M. S., Shalaan, M. T., Alzarie, Y. A., & Zweier, J. L. (2020) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00657.2019 · Cited by 67 · see citing works
Self-citationCellular 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
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
CD38: A Potential Therapeutic Target in Cardiovascular Disease
Zuo, W., Liu, N., Zeng, Y., Liu, Y., Li, B., Wu, K., Xiao, Y., & Liu, Q. (2020) · Cardiovascular Drugs and Therapy · doi:10.1007/s10557-020-07007-8 · Cited by 34 · see citing works
TNB-738, a biparatopic antibody, boosts intracellular NAD+ by inhibiting CD38 ecto-enzyme activity
Ugamraj, H. S., Dang, K. H., Ouisse, L., Buelow, B., Chini, E. N., Castello, G., Allison, J., Clarke, S., Davison, L. M., Buelow, R., et al. (2022) · mAbs · doi:10.1080/19420862.2022.2095949 · Cited by 31 · see citing works
NAD+ and Vascular Dysfunction: From Mechanisms to Therapeutic Opportunities
Abdellatif, M., Bugger, H., Kroemer, G., & Sedej, S. (2022) · Journal of Lipid and Atherosclerosis · doi:10.12997/jla.2022.11.2.111 · Cited by 26 · see citing works
The Emerging Role of Ferroptosis in Sepsis, Opportunity or Challenge?
Huang, Q., Ding, Y., Fang, C., Wang, H., & Kong, L. (2023) · Infection and Drug Resistance · doi:10.2147/idr.s419993 · Cited by 26 · see citing works
NAD metabolism and heart failure: Mechanisms and therapeutic potentials
Walker, M. A., & Tian, R. (2024) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2024.07.008 · Cited by 24 · see citing works
Agorrody, G., Peclat, T., Peluso, G., Gonano, L. A., dos Santos, L. F. V., van Schooten, W., Chini, C. C. S., Escande, C., Chini, E. N., & Contreras, P. (2022) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2022.01.008 · Cited by 23 · see citing works
Lagu, B. R., Wu, X., Kulkarni, S. S., Paul, R., Becherer, J. D., Olson, L., Ravani, S., Chatzianastasiou, A., Papapetropoulos, A., & Andrzejewski, S. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c00688 · Cited by 22 · see citing works
Pathobiochemistry of Aging and Neurodegeneration: Deregulation of NAD+ Metabolism in Brain Cells
Kolotyeva, N. A., Groshkov, A. A., Rozanova, N. A., Berdnikov, A. K., Novikova, S. V., Komleva, Y. K., Salmina, A. B., Illarioshkin, S. N., & Пирадов, М. А. (2024) · Biomolecules · doi:10.3390/biom14121556 · Cited by 22 · see citing works
Fan, Y., Zhao, H., Lu, L., & Wu, W. (2025) · Nutrients · doi:10.3390/nu17111855 · Cited by 19 · see citing works
Yao, W., Liu, M., Li, Z., Qu, L., Sui, S., Xiang, C., Jiang, L., Wang, S., Liu, G., Chen, Y., et al. (2025) · Molecular Therapy · doi:10.1016/j.ymthe.2025.04.039 · Cited by 18 · see citing works
Terpos, E., Stamatelopoulos, K. S., Makris, N., Georgiopoulos, G. A., Ntanasis‐Stathopoulos, I., Gavriatopoulou, M., Laina, A., Eleutherakis‐Papaiakovou, E., Fotiou, D., Kanellias, N., et al. (2021) · Cancers · doi:10.3390/cancers13205057 · Cited by 12 · see citing works
Mohammad, A., Babiker, F. A., & Al‐Bader, M. (2023) · Pharmaceuticals · doi:10.3390/ph16040492 · Cited by 12 · see citing works
Premature senescence and cardiovascular disease following cancer treatments: mechanistic insights
Jain, A., Casanova, D., Padilla, A. V., Paniagua-Bojorges, A., Kotla, S., Ko, K. A., Samanthapudi, V. S. K., Chau, K. M., Nguyen, M. T., Wen, J. J., et al. (2023) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2023.1212174 · Cited by 11 · see citing works
Hannawi, Y., Ewees, M. G., Moore, J. T., & Zweier, J. L. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.881708 · Cited by 11 · see citing works
Self-citationRole of CD38 in Adipose Tissue: Tuning Coenzyme Availability?
Benzi, A., Grozio, A., Spinelli, S., Sturla, L., Guse, A. H., FLORA, A. D., Zocchi, E., Heeren, J., & Bruzzone, S. (2021) · Nutrients · doi:10.3390/nu13113734 · Cited by 10 · see citing works
Banerjee, P., Olmsted‐Davis, E. A., Deswal, A. M., Nguyen, M. T. H., Koutroumpakis, E., Palaskas, N., Lin, S. H., Kotla, S., Reyes‐Gibby, C. C., Yeung, S. J., et al. (2022) · The Journal of Cardiovascular Aging · doi:10.20517/jca.2022.13 · Cited by 10 · see citing works
NAD in pathological cardiac remodeling: Metabolic regulation and beyond
Norambuena‐Soto, I., Deng, Y., Brenner, C., Lavandero, S., & Wang, Z. V. (2024) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2024.167038 · Cited by 9 · see citing works
Mechanism of CD38 via NAD + in the Development of Non-alcoholic Fatty Liver Disease
Dong, M., Wang, S., & Pei, Z. (2023) · International Journal of Medical Sciences · doi:10.7150/ijms.81381 · Cited by 9 · see citing works
CD38 mediates nicotinamide mononucleotide base exchange to yield nicotinic acid mononucleotide
Madawala, R. J., Banks, J. L., Hancock, S. E., Quek, L., Turner, N. A., & Wu, L. E. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.108248 · Cited by 8 · see citing works
Yu, M., Qi, Z., Zhang, J., Zhang, Z., Chen, J., Yan, T., & Chen, Z. (2025) · Journal of Pharmacological Sciences · doi:10.1016/j.jphs.2025.05.013 · Cited by 7 · see citing works
Gouchoe, D. A., Vijayakumar, A., Aly, A. H., Cui, E. Y., Essandoh, M. K., Gumina, R. J., Black, S. M., & Whitson, B. A. (2023) · Journal of Thoracic Disease · doi:10.21037/jtd-23-725 · Cited by 6 · see citing works
The Crucial Role of NAD+ in Mitochondrial Metabolic Regulation
Mishra, K., & Kakhlon, O. (2025) · Biocell · doi:10.32604/biocell.2025.061725 · Cited by 6 · see citing works
NAD+ enhancers as therapeutic agents in the cardiorenal axis
Marin-Blazquez, M., Rovira, J., Ramírez-Bajo, M. J., Perez, R. Z., & Rabadán-Ros, R. (2024) · Cell Communication and Signaling · doi:10.1186/s12964-024-01903-4 · Cited by 6 · see citing works
Harnessing NAD+ Metabolism as Therapy for Cardiometabolic Diseases
Chakraborty, A. D., Minor, K. E., Nizami, H. L., Chiao, Y. A., & Lee, C. F. (2022) · Current Heart Failure Reports · doi:10.1007/s11897-022-00550-5 · Cited by 5 · see citing works
CD38 connects the heart and brain
Tao, Y., Duan, J., Huang, K., Wang, R., Feng, Q., Yang, C., Zhang, X., & Yang, L. (2025) · Translational Psychiatry · doi:10.1038/s41398-025-03597-9 · Cited by 2 · see citing works
Nicotinamide Adenine Dinucleotide and Aging
Jiang, Z., Luo, L., Qin, Y., Huang, Y., & Yan, S. (2025) · Springer eBooks · doi:10.1007/978-981-97-9877-3_28 · Cited by 1 · see citing works
Lin, R., Liang, F., Hu, C., Jiang, L., Wan, Z., Xu, Z., Luo, Y., Ma, J., Wu, Y., Cai, W., et al. (2025) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2025.11.041 · Cited by 1 · see citing works
烟酰胺腺嘌呤二核苷酸（NAD+）合成代谢及其调控机体衰老研究进展
Li, Y., Tian, X., Luo, J., Bao, T., & Wu, X. (2024) · Scientia Sinica Vitae · doi:10.1360/ssv-2024-0004
Research progress in the role of CD38 in clinical tumor treatment.
He, Z., Liu, X., & Zhou, Y. (2022) · PubMed Central · doi:10.11817/j.issn.1672-7347.2022.210351
ENZYMATIC AND ENDOGENOUS SYNTHESIS OF NAD(P)‐DERIVED CALCIUM‐MOBILIZING MESSENGERS
Lee, H. C., & Zhao, Y. J. (2022) · doi:10.1002/9781119692799.ch3
Koju, N., Zhou, M., & Sheng, R. (2025) · Springer eBooks · doi:10.1007/978-981-97-9877-3_37
Repositioning of niacin in atherosclerotic cardiovascular disease
Li, W., Bai, Z., Li, C., Lu, S., Wang, Y., Huang, D., Zhang, H., Yuan, J., Zhen, X., & Liu, Y. (2026) · PharmaNutrition · doi:10.1016/j.phanu.2026.100506
CD38+ NK cells: novel players in immunoregulation
Chang, X., & Fang, K. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1757958
Wang, D., Shi, X., & Zhang, Y. (2026) · Ageing Research Reviews · doi:10.1016/j.arr.2026.103307
Xu, X., Gong, J.-H., Wang, R., Liu, T., Chen, Y.-J., Liu, J.-Y., & Li, J.-Z. (2026) · American Journal of Transplantation · doi:10.1016/j.ajt.2026.09.005
BindingDB Entry 50017291: Orally Bioavailable Enzymatic Inhibitor of CD38,
BindingDB (2023) · UC San Diego · doi:10.7270/q2gb2848
- Authors
- Boslett, J., Reddy, N., Alzarie, Y. A., & Zweier, J. L.
- Affiliations
- The Ohio State University (US)
- Corresponding author
- Zweier, Jay L
- Venue
- The Journal of Pharmacology and Experimental Therapeutics
- Publisher
- Elsevier BV
- Published
- 2019-04
- Volume
- 369
- Issue
- 1
- Pages
- 55-64
- ISSN
- 0022-3565 (ISSN-L)
- PMC
- PMC6413770
- OpenAlex
- W2910447611
- Cited by
- 43
- References
- 45
- Citations by year
- 2026: 4 · 2025: 9 · 2024: 5 · 2023: 6 · 2022: 9 · 2021: 4 · 2020: 5 · 2019: 1
- FWCI
- 3.49
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Pharmacology and Experimental Therapeutics (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Heart, Lung, and Blood Institute (R01HL135648, R01HL131941)
- Topics
- Health Sciences › Medicine › Pathology and Forensic Medicine › Cardiac Ischemia and Reperfusion
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Health Sciences › Medicine › Nephrology › Acute Kidney Injury Research
- Keywords
- myocardial ischemia-reperfusion injury, endothelial nitric oxide synthase, endothelial dysfunction, myocardial infarction, cardiac contractile function, coronary blood flow, high-energy phosphates, tissue permeability, cardioprotection
- MeSH terms
- Animals, Biological Transport, Biopterins, Endothelium, Heart, Mice, Inbred C57BL, Myocardial Contraction, NADP, Quinazolines, Myocardial Reperfusion Injury, Nitric Oxide Synthase, Mice, ADP-ribosyl Cyclase 1, Glycoside Hydrolase Inhibitors
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
