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Nicotinamide Metabolism Mediates Resistance to Venetoclax in Relapsed Acute Myeloid Leukemia Stem Cells

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NAD Metabolism in Cancer Therapeutics

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NAMPT and NAPRT: Two Metabolic Enzymes With Key Roles in Inflammation

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Boosting NAD+ with a small molecule that activates NAMPT

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Beyond Energy Metabolism: Exploiting the Additional Roles of NAMPT for Cancer Therapy

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Retinal Toxicity, in vivo and in vitro, Associated with Inhibition of Nicotinamide Phosphoribosyltransferase

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Nicotinamide Phosphoribosyltransferase Acts as a Metabolic Gate for Mobilization of Myeloid-Derived Suppressor Cells

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Dependence of Tumor Cell Lines and Patient-Derived Tumors on the NAD Salvage Pathway Renders Them Sensitive to NAMPT Inhibition with GNE-618

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Structure-Based Identification of Ureas as Novel Nicotinamide Phosphoribosyltransferase (Nampt) Inhibitors

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NAMPT Is the Cellular Target of STF-31-Like Small-Molecule Probes

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A Preclinical Study on the Rescue of Normal Tissue by Nicotinic Acid in High-Dose Treatment with APO866, a Specific Nicotinamide Phosphoribosyltransferase Inhibitor

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NAD Biosynthesis in Humans - Enzymes, Metabolites and Therapeutic Aspects

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OT-82, a novel anticancer drug candidate that targets the strong dependence of hematological malignancies on NAD biosynthesis

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Depletion of the Central Metabolite NAD Leads to Oncosis-mediated Cell Death

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Next-Generation NAMPT Inhibitors Identified by Sequential High-Throughput Phenotypic Chemical and Functional Genomic Screens

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Temozolomide and Other Potential Agents for the Treatment of Glioblastoma Multiforme

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PPM1D mutations silence NAPRT gene expression and confer NAMPT inhibitor sensitivity in glioma

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A fluorometric assay for high-throughput screening targeting nicotinamide phosphoribosyltransferase

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Selective targeting of NAMPT by KPT-9274 in acute myeloid leukemia

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Advances in NAD-Lowering Agents for Cancer Treatment

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Extensive regulation of nicotinate phosphoribosyltransferase (NAPRT) expression in human tissues and tumors

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

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Supplementation of Nicotinic Acid with NAMPT Inhibitors Results in Loss of In Vivo Efficacy in NAPRT1-Deficient Tumor Models

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Identification of Novel Triazole-Based Nicotinamide Phosphoribosyltransferase (NAMPT) Inhibitors Endowed with Antiproliferative and Antiinflammatory Activity

Travelli, C., Aprile, S., Rahimian, R., Grolla, A. A., Rogati, F., Bertolotti, M., Malagnino, F., Paola, R. D., Impellizzeri, D., Fusco, R., et al. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b01392 · Cited by 61

Dynamics of NAD-metabolism: everything but constant

Opitz, C. A., & Heiland, I. (2015) · Biochemical Society Transactions · doi:10.1042/bst20150133 · Cited by 58

Targeting Metabolic Changes in Cancer: Novel Therapeutic Approaches

Bobrovnikova-Marjon, E. V., & Hurov, J. (2014) · Annual Review of Medicine · doi:10.1146/annurev-med-092012-112344 · Cited by 56

Inhibitor of Nicotinamide Phosphoribosyltransferase Sensitizes Glioblastoma Cells to Temozolomide via Activating ROS/JNK Signaling Pathway

Feng, J., Yan, P.-F., Zhao, H., Zhang, F., Zhao, W., & Feng, M. (2016) · BioMed Research International · doi:10.1155/2016/1450843 · Cited by 53

Inhibition of Nicotinamide Phosphoribosyltransferase (NAMPT), an Enzyme Essential for NAD+ Biosynthesis, Leads to Altered Carbohydrate Metabolism in Cancer Cells

Tan, B., Dong, S., Shepard, R. L., Kays, L. M., Roth, K. D. W., Geeganage, S., Kuo, M., & Zhao, G. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.632141 · Cited by 54

Nicotinamide Phosphoribosyl Transferase (Nampt) Is Required for De Novo Lipogenesis in Tumor Cells

Bowlby, S. C., Thomas, M. J., D’Agostino, R. B., & Kridel, S. J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0040195 · Cited by 54

Chemical Proteomics Identifies Nampt as the Target of CB30865, An Orphan Cytotoxic Compound

Fleischer, T. C., Murphy, B. R., Flick, J. S., Terry-Lorenzo, R. T., Gao, Z.-H., Davis, T., McKinnon, R. S., Ostanin, K., Willardsen, J. A., & Boniface, J. J. (2010) · Chemistry & Biology · doi:10.1016/j.chembiol.2010.05.008 · Cited by 54

Nicotinamide adenine dinucleotide (NAD+): essential redox metabolite, co-substrate and an anti-cancer and anti-ageing therapeutic target

Griffiths, H. B. S., Williams, C., King, S. J., & Allison, S. J. (2020) · Biochemical Society Transactions · doi:10.1042/bst20190033 · Cited by 57

Target enzyme mutations are the molecular basis for resistance towards pharmacological inhibition of nicotinamide phosphoribosyltransferase

Olesen, U. H., Petersen, J. G., Garten, A., Kieß, W., Yoshino, J., Imai, S., Christensen, M. K., Fristrup, P., Thougaard, A., Björkling, F., et al. (2010) · BMC Cancer · doi:10.1186/1471-2407-10-677 · Cited by 53

New strategies to maximize therapeutic opportunities for NAMPT inhibitors in oncology

Roulston, A., & Shore, G. C. (2015) · Molecular & Cellular Oncology · doi:10.1080/23723556.2015.1052180 · Cited by 54

Metabolomics as a Key Integrator for “Omic” Advancement of Personalized Medicine and Future Therapies

Eckhart, A. D., Beebe, K. D., & Milburn, M. (2012) · Clinical and Translational Science · doi:10.1111/j.1752-8062.2011.00388.x · Cited by 52

Structural and Biochemical Analyses of the Catalysis and Potency Impact of Inhibitor Phosphoribosylation by Human Nicotinamide Phosphoribosyltransferase

Oh, A., Ho, Y., Zak, M., Liu, Y., Chen, X., Yuen, P., Zheng, X., Liu, Y., Dragovich, P. S., & Wang, W. (2014) · ChemBioChem · doi:10.1002/cbic.201402023 · Cited by 51

Targeted Delivery of Cytotoxic NAMPT Inhibitors Using Antibody–Drug Conjugates

Neumann, C. S., Olivas, K. C., Anderson, M. E., Cochran, J. H., Jin, S., Li, F., Loftus, L. V., Meyer, D. W., Neale, J. R., Nix, J. C., et al. (2018) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-18-0643 · Cited by 51

Recycling Nicotinamide. The Transition-State Structure of Human Nicotinamide Phosphoribosyltransferase

Burgos, E. S., Vetticatt, M. J., & Schramm, V. L. (2013) · Journal of the American Chemical Society · doi:10.1021/ja310180c · Cited by 50

Cancer cell metabolic plasticity allows resistance to NAMPT inhibition but invariably induces dependence on LDHA

Thongon, N., Zucal, C., D’Agostino, V., Tebaldi, T., Ravera, S., Zamporlini, F., Piacente, F., Moschoi, R., Raffaelli, N., Quattrone, A., et al. (2018) · Cancer & Metabolism · doi:10.1186/s40170-018-0174-7 · Cited by 51

Identification of amides derived from 1H-pyrazolo[3,4-b]pyridine-5-carboxylic acid as potent inhibitors of human nicotinamide phosphoribosyltransferase (NAMPT)

Zheng, X., Bair, K. W., Bauer, P., Baumeister, T., Bowman, K. K., Buckmelter, A. J., Caligiuri, M., Clodfelter, K. H., Feng, Y., Han, B., et al. (2013) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2013.08.074 · Cited by 49

Novel assay for simultaneous measurement of pyridine mononucleotides synthesizing activities allows dissection of the NAD + biosynthetic machinery in mammalian cells

Zamporlini, F., Ruggieri, S., Mazzola, F., Amici, A., Orsomando, G., & Raffaelli, N. (2014) · FEBS Journal · doi:10.1111/febs.13050 · Cited by 48

Software Techniques for Enabling High-Throughput Analysis of Metabolomic Datasets

Corey, D., Anne, M., Dai, H., & Khutorskaya, I. A. (2012) · InTech eBooks · doi:10.5772/31277 · Cited by 48

Synergy between the NAMPT inhibitor GMX1777(8) and pemetrexed in non-small cell lung cancer cells is mediated by PARP activation and enhanced NAD consumption

Chan, M., Gravel, M., Bramoullé, A., Bridon, G., Avizonis, D., Shore, G. C., & Roulston, A. (2014) · Cancer Research · doi:10.1158/0008-5472.can-14-0809 · Cited by 46

Discovery of a Highly Selective NAMPT Inhibitor That Demonstrates Robust Efficacy and Improved Retinal Toxicity with Nicotinic Acid Coadministration

Zhao, G., Green, C. F., Hui, Y., Prieto, L., Shepard, R. L., Dong, S., Wang, T., Tan, B., Gong, X., Kays, L. M., et al. (2017) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-16-0674 · Cited by 46

Research into cancer metabolomics: Towards a clinical metamorphosis

Olivares, O., Däbritz, J. H. M., King, A., Gottlieb, E., & Halsey, C. (2015) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2015.09.008 · Cited by 45

Nicotinamide Phosphoribosyltransferase Inhibitors, Design, Preparation, and Structure–Activity Relationship

Christensen, M. K., Erichsen, K. D., Olesen, U. H., Tjørnelund, J., Fristrup, P., Thougaard, A., Nielsen, S. J., Sehested, M., Jensen, P. B., Loža, E., et al. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm4009949 · Cited by 44

Fragment-Based Identification of Amides Derived from trans-2-(Pyridin-3-yl)cyclopropanecarboxylic Acid as Potent Inhibitors of Human Nicotinamide Phosphoribosyltransferase (NAMPT)

Giannetti, A. M., Zheng, X., Skelton, N. J., Wang, W., Bravo, B. J., Bair, K. W., Baumeister, T., Cheng, E., Crocker, L., Feng, Y., et al. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm4015108 · Cited by 44

Minimizing CYP2C9 Inhibition of Exposed-Pyridine NAMPT (Nicotinamide Phosphoribosyltransferase) Inhibitors

Zak, M., Yuen, P., Liu, X., Patel, S. D., Sampath, D., Oeh, J., Liederer, B. M., Wang, W., O’Brien, T., Xiao, Y., et al. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b00697 · Cited by 44

Discovery of potent and efficacious urea-containing nicotinamide phosphoribosyltransferase (NAMPT) inhibitors with reduced CYP2C9 inhibition properties

Gunzner, J. L., Zhao, G., Bauer, P., Baumeister, T., Buckmelter, A. J., Caligiuri, M., Clodfelter, K. H., Fu, B., Han, B., Ho, Y., et al. (2013) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2013.04.040 · Cited by 43

NAD Synthesis Pathway Interference Is a Viable Therapeutic Strategy for Chondrosarcoma

Peterse, E. F. P., van den Akker, B. E. W. M., Niessen, B., Oosting, J., Suijker, J., de Jong, Y., Danen, E. H. J., Cleton-Jansen, A., & Bovée, J. V. M. G. (2017) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-17-0293 · Cited by 43

Nicotinamide Phosphoribosyltransferase: A Potent Therapeutic Target in Non-small Cell Lung Cancer with Epidermal Growth Factor Receptor-Gene Mutation

Okumura, S., Sasaki, T., Minami, Y., & Ohsaki, Y. (2011) · Journal of Thoracic Oncology · doi:10.1097/jto.0b013e318233d686 · Cited by 43

The Small Molecule GMX1778 Is a Potent Inhibitor of NAD Biosynthesis: Strategy for Enhanced Therapy in Nicotinic Acid

Tumors, P. D., Shore, G. C., & Beauparlant, P. (2009)

NAPRT1 and p53 Status in Cancer and Normal Cells Modulate Induction of ROS Induced by GMX1777/1778: Implication for Synthetic Lethality in Tumors Defective in NAPRT1 and p53

Yoo, S., Cerna, D., Li, H., Flaherty, S. M., Takebe, N., & Coleman, C. N. (2010) · International Journal of Radiation Oncology*Biology*Physics · doi:10.1016/j.ijrobp.2010.07.1527 · Cited by 1

GMX1777: a novel inhibitor of NAD+ biosynthesis via inhibition of nicotinamide phosphoribosyl transferase.

Roulston, A., Watson, M. H., Bernier, C., Chan, H. H. L., Gratton, M., Jang, A., Koch, E. M., Lavoie, M., Paquette, D., Mitchell, M. W., et al. (2007) · Molecular Cancer Therapeutics · Cited by 3

Abstract B98: Induction of metabolic and oxidative stresses by the novel inhibitor of NAD+ biosynthesis, GMX 1778, for specific killing of human glioblastomas

Yoo, S. S., Cerna, D., Carter, D. J., Flaherty, S. M., Li, H., Takebe, N., & Watson, M. H. (2009) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.targ-09-b98

Abstract 2127: Identification of a novel NAMPT inhibition resistance mechanism utilizing the de novo NAD+ biosynthesis pathway

Guo, J. Q., Tse, C., & Pappano, W. N. (2016) · Cancer Research · doi:10.1158/1538-7445.am2016-2127