CoChat
Sign Up
Cited by 68Sirtuins and Resveratrol in MedicineBiochemical and Molecular ResearchCalcium signaling and nucleotide metabolism

Nicotinamide Adenine Dinucleotide (NAD) Metabolism as a Relevant Target in Cancer

Open access
Navas, Lola E., Carnero, Amancio·2022·Cells
DOI 10.3390/cells11172627PMC PMC9454445
Open this paper in CoChat — free account

Abstract

NAD+ is an important metabolite in cell homeostasis that acts as an essential cofactor in oxidation–reduction (redox) reactions in various energy production processes, such as the Krebs cycle, fatty acid oxidation, glycolysis and serine biosynthesis. Furthermore, high NAD+ levels are required since they also participate in many other nonredox molecular processes, such as DNA repair, posttranslational modifications, cell signalling, senescence, inflammatory responses and apoptosis. In these nonredox reactions, NAD+ is an ADP-ribose donor for enzymes such as sirtuins (SIRTs), poly-(ADP-ribose) polymerases (PARPs) and cyclic ADP-ribose (cADPRs). Therefore, to meet both redox and nonredox NAD+ demands, tumour cells must maintain high NAD+ levels, enhancing their synthesis mainly through the salvage pathway. NAMPT, the rate-limiting enzyme of this pathway, has been identified as an oncogene in some cancer types. Thus, NAMPT has been proposed as a suitable target for cancer therapy. NAMPT inhibition causes the depletion of NAD+ content in the cell, leading to the inhibition of ATP synthesis. This effect can cause a decrease in tumour cell proliferation and cell death, mainly by apoptosis. Therefore, in recent years, many specific inhibitors of NAMPT have been developed, and some of them are currently in clinical trials. Here we review the NAD metabolism as a cancer therapy target.

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.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.3390/cells11172627

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.

A few free checks a day · papers already verified open instantly · results are public

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?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

The citation lists haven’t been fetched yet

References 161 · Cited by 68

Research works printed but not linked: 153

  1. [1]Navas L.E. Carnero A. NAD(+) metabolism, stemness, the immune response, and cancer Signal Transduct. Target Ther. 2021 6 2 10.1038/s41392-020-00354-w 33384409 PMC7775471 · DOI
  2. [2]Poljsak B. NAD+ in Cancer Prevention and Treatment: Pros and Cons J. Clin. Exp. Oncol. 2016 4 2 10.4172/2324-9110.1000165 · DOI
  3. [3]Yang Y. Sauve A.A. NAD(+) metabolism: Bioenergetics, signaling and manipulation for therapy Biochim. Biophys. Acta 2016 1864 1787 1800 10.1016/j.bbapap.2016.06.014 27374990 PMC5521000 · DOI
  4. [4]Nakamura M. Bhatnagar A. Sadoshima J. Overview of pyridine nucleotides review series Circ. Res. 2012 111 604 610 10.1161/CIRCRESAHA.111.247924 22904040 PMC3523884 · DOI
  5. [5]Guillot B. Lecomte C. Cousson A. Scherf C. Jelsch C. High-resolution neutron structure of nicotinamide adenine dinucleotide Acta Crystallogr. D. Biol. Crystallogr. 2001 57 981 989 10.1107/S0907444901007120 11418766 · DOI
  6. [6]Htet Y. Tennyson A.G. NAD(+) as a Hydride Donor and Reductant J. Am. Chem. Soc. 2016 138 15833 15836 10.1021/jacs.6b10451 27960347 · DOI
  7. [7]Fletcher R.S. Lavery G.G. The emergence of the nicotinamide riboside kinases in the regulation of NAD+ metabolism J. Mol. Endocrinol. 2018 61 R107 R121 10.1530/JME-18-0085 30307159 PMC6145238 · DOI
  8. [8]Kulkarni C.A. Brookes P.S. Cellular Compartmentation and the Redox/Nonredox Functions of NAD(+) Antioxid. Redox Signal 2019 31 623 642 10.1089/ars.2018.7722 30784294 PMC6657305 · DOI
  9. [9]Opitz C.A. Heiland I. Dynamics of NAD-metabolism: Everything but constant Biochem. Soc. Trans. 2015 43 1127 1132 10.1042/BST20150133 26614649 · DOI
  10. [10]Nakahata Y. Sahar S. Astarita G. Kaluzova M. Sassone-Corsi P. Circadian control of the NAD+ salvage pathway by CLOCK-SIRT1 Science 2009 324 654 657 10.1126/science.1170803 19286518 PMC6501775 · DOI · Paper page
  11. [11]Masri S. Sirtuin-dependent clock control: New advances in metabolism, aging and cancer Curr. Opin. Clin. Nutr. Metab. Care 2015 18 521 527 10.1097/MCO.0000000000000219 26335311 PMC4610809 · DOI
  12. [12]Ramsey K.M. Yoshino J. Brace C.S. Abrassart D. Kobayashi Y. Marcheva B. Hong H.K. Chong J.L. Buhr E.D. Lee C. Circadian clock feedback cycle through NAMPT-mediated NAD+ biosynthesis Science 2009 324 651 654 10.1126/science.1171641 19299583 PMC2738420 · DOI · Paper page
  13. [13]Carracedo A. Cantley L.C. Pandolfi P.P. Cancer metabolism: Fatty acid oxidation in the limelight Nat. Rev. Cancer 2013 13 227 232 10.1038/nrc3483 23446547 PMC3766957 · DOI
  14. [14]Dan Dunn J. Alvarez L.A. Zhang X. Soldati T. Reactive oxygen species and mitochondria: A nexus of cellular homeostasis Redox Biol. 2015 6 472 485 10.1016/j.redox.2015.09.005 26432659 PMC4596921 · DOI
  15. [15]Lee B.W.L. Ghode P. Ong D.S.T. Redox regulation of cell state and fate Redox Biol. 2019 25 101056 10.1016/j.redox.2018.11.014 30509603 PMC6859564 · DOI
  16. [16]Chiarugi A. Dolle C. Felici R. Ziegler M. The NAD metabolome—A key determinant of cancer cell biology Nat. Rev. Cancer 2012 12 741 752 10.1038/nrc3340 23018234 · DOI
  17. [17]Braidy N. Berg J. Clement J. Khorshidi F. Poljak A. Jayasena T. Grant R. Sachdev P. Role of Nicotinamide Adenine Dinucleotide and Related Precursors as Therapeutic Targets for Age-Related Degenerative Diseases: Rationale, Biochemistry, Pharmacokinetics, and Outcomes Antioxid. Redox Signal 2019 30 251 294 10.1089/ars.2017.7269 29634344 PMC6277084 · DOI
  18. [19]Rajman L. Chwalek K. Sinclair D.A. Therapeutic Potential of NAD-Boosting Molecules: The In Vivo Evidence Cell Metab. 2018 27 529 547 10.1016/j.cmet.2018.02.011 29514064 PMC6342515 · DOI · Paper page
  19. [20]Kim M.Y. Zhang T. Kraus W.L. Poly(ADP-ribosyl)ation by PARP-1: ‘PAR-laying’ NAD+ into a nuclear signal Genes Dev. 2005 19 1951 1967 10.1101/gad.1331805 16140981 · DOI
  20. [21]Langelier M.F. Zandarashvili L. Aguiar P.M. Black B.E. Pascal J.M. NAD(+) analog reveals PARP-1 substrate-blocking mechanism and allosteric communication from catalytic center to DNA-binding domains Nat. Commun. 2018 9 844 10.1038/s41467-018-03234-8 29487285 PMC5829251 · DOI
  21. [22]Houtkooper R.H. Canto C. Wanders R.J. Auwerx J. The secret life of NAD+: An old metabolite controlling new metabolic signaling pathways Endocr. Rev. 2010 31 194 223 10.1210/er.2009-0026 20007326 PMC2852209 · DOI · Paper page
  22. [24]Gomes A.P. Price N.L. Ling A.J. Moslehi J.J. Montgomery M.K. Rajman L. White J.P. Teodoro J.S. Wrann C.D. Hubbard B.P. Declining NAD(+) induces a pseudohypoxic state disrupting nuclear-mitochondrial communication during aging Cell 2013 155 1624 1638 10.1016/j.cell.2013.11.037 24360282 PMC4076149 · DOI · Paper page
  23. [25]Moreschi I. Bruzzone S. Melone L. De Flora A. Zocchi E. NAADP+ synthesis from cADPRP and nicotinic acid by ADP-ribosyl cyclases Biochem. Biophys. Res. Commun. 2006 345 573 580 10.1016/j.bbrc.2006.04.096 16690024 · DOI
  24. [26]Hanahan D. Weinberg R.A. Hallmarks of cancer: The next generation Cell 2011 144 646 674 10.1016/j.cell.2011.02.013 21376230 · DOI · Paper page
  25. [27]Moreira J.D. Hamraz M. Abolhassani M. Bigan E. Peres S. Pauleve L. Nogueira M.L. Steyaert J.M. Schwartz L. The Redox Status of Cancer Cells Supports Mechanisms behind the Warburg Effect Metabolites 2016 6 33 10.3390/metabo6040033 PMC5192439 27706102 · DOI
  26. [28]Liberti M.V. Locasale J.W. The Warburg Effect: How Does it Benefit Cancer Cells? Trends Biochem. Sci. 2016 41 211 218 10.1016/j.tibs.2015.12.001 26778478 PMC4783224 · DOI · Paper page
  27. [29]Cantor J.R. Sabatini D.M. Cancer cell metabolism: One hallmark, many faces Cancer Discov. 2012 2 881 898 10.1158/2159-8290.CD-12-0345 23009760 PMC3491070 · DOI
  28. [30]Yaku K. Okabe K. Hikosaka K. Nakagawa T. NAD Metabolism in Cancer Therapeutics Front. Oncol. 2018 8 622 10.3389/fonc.2018.00622 30631755 PMC6315198 · DOI
  29. [31]DeBerardinis R.J. Lum J.J. Hatzivassiliou G. Thompson C.B. The biology of cancer: Metabolic reprogramming fuels cell growth and proliferation Cell Metab. 2008 7 11 20 10.1016/j.cmet.2007.10.002 18177721 · DOI · Paper page
  30. [32]Mates J.M. Di Paola F.J. Campos-Sandoval J.A. Mazurek S. Marquez J. Therapeutic targeting of glutaminolysis as an essential strategy to combat cancer Semin. Cell Dev. Biol. 2020 98 34 43 10.1016/j.semcdb.2019.05.012 31100352 · DOI
  31. [33]Bott A.J. Maimouni S. Zong W.X. The Pleiotropic Effects of Glutamine Metabolism in Cancer Cancers 2019 11 770 10.3390/cancers11060770 31167399 PMC6627534 · DOI
  32. [34]Patra K.C. Hay N. The pentose phosphate pathway and cancer Trends Biochem. Sci. 2014 39 347 354 10.1016/j.tibs.2014.06.005 25037503 PMC4329227 · DOI
  33. [35]Amelio I. Cutruzzola F. Antonov A. Agostini M. Melino G. Serine and glycine metabolism in cancer Trends Biochem. Sci. 2014 39 191 198 10.1016/j.tibs.2014.02.004 24657017 PMC3989988 · DOI
  34. [36]Mattaini K.R. Sullivan M.R. Vander Heiden M.G. The importance of serine metabolism in cancer J. Cell Biol. 2016 214 249 257 10.1083/jcb.201604085 27458133 PMC4970329 · DOI
  35. [37]Cambronne X.A. Stewart M.L. Kim D. Jones-Brunette A.M. Morgan R.K. Farrens D.L. Cohen M.S. Goodman R.H. Biosensor reveals multiple sources for mitochondrial NAD(+) Science 2016 352 1474 1477 10.1126/science.aad5168 27313049 PMC6530784 · DOI · Paper page
  36. [38]Hara N. Yamada K. Terashima M. Osago H. Shimoyama M. Tsuchiya M. Molecular identification of human glutamine- and ammonia-dependent NAD synthetases. Carbon-nitrogen hydrolase domain confers glutamine dependency J. Biol. Chem. 2003 278 10914 10921 10.1074/jbc.M209203200 12547821 · DOI
  37. [39]Lucena-Cacace A. Carnero A. Nicotinamide phosphoribosyltransferase: Biology, role in cancer, and novel drug target Cancer Transl. Med. 2018 4 109 116 10.4103/ctm.ctm_20_18 · DOI
  38. [40]Lucena-Cacace A. Otero-Albiol D. Jimenez-Garcia M.P. Munoz-Galvan S. Carnero A. NAMPT Is a Potent Oncogene in Colon Cancer Progression that Modulates Cancer Stem Cell Properties and Resistance to Therapy through Sirt1 and PARP Clin. Cancer Res. 2018 24 1202 1215 10.1158/1078-0432.CCR-17-2575 29203587 · DOI
  39. [41]Lucena-Cacace A. Otero-Albiol D. Jimenez-Garcia M.P. Peinado-Serrano J. Carnero A. NAMPT overexpression induces cancer stemness and defines a novel tumor signature for glioma prognosis Oncotarget 2017 8 99514 99530 10.18632/oncotarget.20577 29245920 PMC5725111 · DOI
  40. [43]Lucena-Cacace A. Umeda M. Navas L.E. Carnero A. NAMPT as a Dedifferentiation-Inducer Gene: NAD(+) as Core Axis for Glioma Cancer Stem-Like Cells Maintenance Front. Oncol. 2019 9 292 10.3389/fonc.2019.00292 31119097 PMC6507617 · DOI
  41. [45]Wu L.E. Sinclair D.A. The elusive NMN transporter is found Nat. Metab. 2019 1 8 9 10.1038/s42255-018-0015-6 32694812 · DOI
  42. [46]Wang Y.Y. Hung A.C. Lo S. Yuan S.F. Adipocytokines visfatin and resistin in breast cancer: Clinical relevance, biological mechanisms, and therapeutic potential Cancer Lett. 2021 498 229 239 10.1016/j.canlet.2020.10.045 33152400 · DOI
  43. [47]Grolla A.A. Travelli C. Genazzani A.A. Sethi J.K. Extracellular nicotinamide phosphoribosyltransferase, a new cancer metabokine Br. J. Pharmacol. 2016 173 2182 2194 10.1111/bph.13505 27128025 PMC4919578 · DOI
  44. [48]Sun Z. Lei H. Zhang Z. Pre-B cell colony enhancing factor (PBEF), a cytokine with multiple physiological functions Cytokine Growth Factor Rev. 2013 24 433 442 10.1016/j.cytogfr.2013.05.006 23787158 PMC3791181 · DOI
  45. [49]Ognjanovic S. Bao S. Yamamoto S.Y. Garibay-Tupas J. Samal B. Bryant-Greenwood G.D. Genomic organization of the gene coding for human pre-B-cell colony enhancing factor and expression in human fetal membranes J. Mol. Endocrinol. 2001 26 107 117 10.1677/jme.0.0260107 11241162 · DOI
  46. [50]Samal B. Sun Y. Stearns G. Xie C. Suggs S. McNiece I. Cloning and characterization of the cDNA encoding a novel human pre-B-cell colony-enhancing factor Mol. Cell Biol. 1994 14 1431 1437 10.1128/mcb.14.2.1431-1437.1994 8289818 PMC358498 · DOI
  47. [52]Dakroub A. Nasser S.A. Younis N. Bhagani H. Al-Dhaheri Y. Pintus G. Eid A.A. El-Yazbi A.F. Eid A.H. Visfatin: A Possible Role in Cardiovasculo-Metabolic Disorders Cells 2020 9 2444 10.3390/cells9112444 33182523 PMC7696687 · DOI
  48. [53]Zhang L.Q. Heruth D.P. Ye S.Q. Nicotinamide Phosphoribosyltransferase in Human Diseases J. Bioanal Biomed. 2011 3 13 25 10.4172/1948-593X.1000038 22140607 PMC3227030 · DOI
  49. [54]Chen H. Xia T. Zhou L. Chen X. Gan L. Yao W. Peng Y. Yang Z. Gene organization, alternate splicing and expression pattern of porcine visfatin gene Domest. Anim. Endocrinol. 2007 32 235 245 10.1016/j.domaniend.2006.03.004 16857338 · DOI
  50. [55]Takahashi R. Nakamura S. Nakazawa T. Minoura K. Yoshida T. Nishi Y. Kobayashi Y. Ohkubo T. Structure and reaction mechanism of human nicotinamide phosphoribosyltransferase J. Biochem. 2010 147 95 107 10.1093/jb/mvp152 19819904 · DOI
  51. [56]Dulyaninova N.G. Podlepa E.M. Toulokhonova L.V. Bykhovsky V.Y. Salvage pathway for NAD biosynthesis in Brevibacterium ammoniagenes: Regulatory properties of triphosphate-dependent nicotinate phosphoribosyltransferase Biochim. Biophys. Acta 2000 1478 211 220 10.1016/S0167-4838(00)00045-5 10825532 · DOI
  52. [57]Kim M.K. Lee J.H. Kim H. Park S.J. Kim S.H. Kang G.B. Lee Y.S. Kim J.B. Kim K.K. Suh S.W. Crystal structure of visfatin/pre-B cell colony-enhancing factor 1/nicotinamide phosphoribosyltransferase, free and in complex with the anti-cancer agent FK-866 J. Mol. Biol 2006 362 66 77 10.1016/j.jmb.2006.06.082 16901503 · DOI
  53. [58]Wang T. Zhang X. Bheda P. Revollo J.R. Imai S. Wolberger C. Structure of Nampt/PBEF/visfatin, a mammalian NAD+ biosynthetic enzyme Nat. Struct. Mol. Biol. 2006 13 661 662 10.1038/nsmb1114 16783373 · DOI
  54. [59]Khan J.A. Tao X. Tong L. Molecular basis for the inhibition of human NMPRTase, a novel target for anticancer agents Nat. Struct. Mol. Biol. 2006 13 582 588 10.1038/nsmb1105 16783377 · DOI
  55. [60]Burgos E.S. Ho M.C. Almo S.C. Schramm V.L. A phosphoenzyme mimic, overlapping catalytic sites and reaction coordinate motion for human NAMPT Proc. Natl. Acad. Sci. USA 2009 106 13748 13753 10.1073/pnas.0903898106 19666527 PMC2728965 · DOI
  56. [61]Burgos E.S. Schramm V.L. Weak coupling of ATP hydrolysis to the chemical equilibrium of human nicotinamide phosphoribosyltransferase Biochemistry 2008 47 11086 11096 10.1021/bi801198m 18823127 PMC2657875 · DOI
  57. [62]Bi T.Q. Che X.M. Nampt/PBEF/visfatin and cancer Cancer Biol. Ther. 2010 10 119 125 10.4161/cbt.10.2.12581 20647743 · DOI
  58. [63]Olesen U.H. Hastrup N. Sehested M. Expression patterns of nicotinamide phosphoribosyltransferase and nicotinic acid phosphoribosyltransferase in human malignant lymphomas APMIS 2011 119 296 303 10.1111/j.1600-0463.2011.02733.x 21492230 · DOI
  59. [64]Wang B. Hasan M.K. Alvarado E. Yuan H. Wu H. Chen W.Y. NAMPT overexpression in prostate cancer and its contribution to tumor cell survival and stress response Oncogene 2011 30 907 921 10.1038/onc.2010.468 20956937 · DOI
  60. [65]Zhang H. Zhang N. Liu Y. Su P. Liang Y. Li Y. Wang X. Chen T. Song X. Sang Y. Epigenetic Regulation of NAMPT by NAMPT-AS Drives Metastatic Progression in Triple-Negative Breast Cancer Cancer Res. 2019 79 3347 3359 10.1158/0008-5472.CAN-18-3418 30940661 · DOI
  61. [66]Sawicka-Gutaj N. Waligorska-Stachura J. Andrusiewicz M. Biczysko M. Sowinski J. Skrobisz J. Ruchala M. Nicotinamide phosphorybosiltransferase overexpression in thyroid malignancies and its correlation with tumor stage and with survivin/survivin DEx3 expression Tumour Biol. 2015 36 7859 7863 10.1007/s13277-015-3506-z 25946974 PMC4605962 · DOI
  62. [67]Bi T.Q. Che X.M. Liao X.H. Zhang D.J. Long H.L. Li H.J. Zhao W. Overexpression of Nampt in gastric cancer and chemopotentiating effects of the Nampt inhibitor FK866 in combination with fluorouracil Oncol. Rep. 2011 26 1251 1257 10.3892/or.2011.1378 21743967 · DOI
  63. [68]Kim J.Y. Bae Y.H. Bae M.K. Kim S.R. Park H.J. Wee H.J. Bae S.K. Visfatin through STAT3 activation enhances IL-6 expression that promotes endothelial angiogenesis Biochim. Biophys. Acta 2009 1793 1759 1767 10.1016/j.bbamcr.2009.09.006 19751774 · DOI
  64. [69]Kim S.R. Bae Y.H. Bae S.K. Choi K.S. Yoon K.H. Koo T.H. Jang H.O. Yun I. Kim K.W. Kwon Y.G. Visfatin enhances ICAM-1 and VCAM-1 expression through ROS-dependent NF-kappaB activation in endothelial cells Biochim. Biophys. Acta 2008 1783 886 895 10.1016/j.bbamcr.2008.01.004 18241674 · DOI
  65. [70]Cymbaluk-Ploska A. Chudecka-Glaz A. Pius-Sadowska E. Sompolska-Rzechula A. Machalinski B. Menkiszak J. Circulating Serum Level of Visfatin in Patients with Endometrial Cancer Biomed. Res. Int. 2018 2018 8576179 10.1155/2018/8576179 29516012 PMC5817356 · DOI
  66. [71]Pazgan-Simon M. Kukla M. Zuwala-Jagiello J. Derra A. Bator M. Menzyk T. Lekstan A. Grzebyk E. Simon K. Serum visfatin and vaspin levels in hepatocellular carcinoma (HCC) PLoS ONE 2020 15 e0227459 10.1371/journal.pone.0227459 31935230 PMC6959555 · DOI
  67. [72]Lu G.W. Wang Q.J. Xia M.M. Qian J. Elevated plasma visfatin levels correlate with poor prognosis of gastric cancer patients Peptides 2014 58 60 64 10.1016/j.peptides.2014.05.016 24911837 · DOI
  68. [73]Lin T.C. The role of visfatin in cancer proliferation, angiogenesis, metastasis, drug resistance and clinical prognosis Cancer Manag. Res. 2019 11 3481 3491 10.2147/CMAR.S199597 31114381 PMC6497876 · DOI
  69. [74]Lu Y.B. Chen C.X. Huang J. Tian Y.X. Xie X. Yang P. Wu M. Tang C. Zhang W.P. Nicotinamide phosphoribosyltransferase secreted from microglia via exosome during ischemic injury J. Neurochem. 2019 150 723 737 10.1111/jnc.14811 31269239 · DOI · Paper page
  70. [75]Audrito V. Messana V.G. Brandimarte L. Deaglio S. The Extracellular NADome Modulates Immune Responses Front. Immunol. 2021 12 704779 10.3389/fimmu.2021.704779 34421911 PMC8371318 · DOI
  71. [76]Vona-Davis L. Rose D.P. Adipokines as endocrine, paracrine, and autocrine factors in breast cancer risk and progression Endocr. Relat. Cancer 2007 14 189 206 10.1677/ERC-06-0068 17639037 · DOI · Paper page
  72. [77]Wang Y.Y. Chen H.D. Lo S. Chen Y.K. Huang Y.C. Hu S.C. Hsieh Y.C. Hung A.C. Hou M.F. Yuan S.F. Visfatin Enhances Breast Cancer Progression through CXCL1 Induction in Tumor-Associated Macrophages Cancers 2020 12 3526 10.3390/cancers12123526 PMC7760195 33256011 · DOI
  73. [78]Li Y. Zhang Y. Dorweiler B. Cui D. Wang T. Woo C.W. Brunkan C.S. Wolberger C. Imai S. Tabas I. Extracellular Nampt promotes macrophage survival via a nonenzymatic interleukin-6/STAT3 signaling mechanism J. Biol. Chem. 2008 283 34833 34843 10.1074/jbc.M805866200 18945671 PMC2596403 · DOI
  74. [79]Aman Y. Qiu Y. Tao J. Fang E.F. Therapeutic potential of boosting NAD+ in aging and age-related diseases Transl. Med. Aging 2018 2 30 37 10.1016/j.tma.2018.08.003 · DOI
  75. [80]Hwang E.S. Song S.B. Nicotinamide is an inhibitor of SIRT1 in vitro, but can be a stimulator in cells Cell Mol. Life Sci. 2017 74 3347 3362 10.1007/s00018-017-2527-8 28417163 PMC11107671 · DOI
  76. [81]Menssen A. Hydbring P. Kapelle K. Vervoorts J. Diebold J. Luscher B. Larsson L.G. Hermeking H. The c-MYC oncoprotein, the NAMPT enzyme, the SIRT1-inhibitor DBC1, and the SIRT1 deacetylase form a positive feedback loop Proc. Natl. Acad. Sci. USA 2012 109 E187 E196 10.1073/pnas.1105304109 22190494 PMC3268300 · DOI
  77. [82]Behrouzfar K. Alaee M. Nourbakhsh M. Gholinejad Z. Golestani A. Extracellular NAMPT/visfatin causes p53 deacetylation via NAD production and SIRT1 activation in breast cancer cells Cell Biochem. Funct. 2017 35 327 333 10.1002/cbf.3279 28845527 · DOI
  78. [83]Kennedy B.E. Sharif T. Martell E. Dai C. Kim Y. Lee P.W. Gujar S.A. NAD(+) salvage pathway in cancer metabolism and therapy Pharmacol. Res. 2016 114 274 283 10.1016/j.phrs.2016.10.027 27816507 · DOI
  79. [84]Wang L. Liang C. Li F. Guan D. Wu X. Fu X. Lu A. Zhang G. PARP1 in Carcinomas and PARP1 Inhibitors as Antineoplastic Drugs Int. J. Mol. Sci. 2017 18 2111 10.3390/ijms18102111 PMC5666793 28991194 · DOI
  80. [85]Dorsam B. Seiwert N. Foersch S. Stroh S. Nagel G. Begaliew D. Diehl E. Kraus A. McKeague M. Minneker V. PARP-1 protects against colorectal tumor induction, but promotes inflammation-driven colorectal tumor progression Proc. Natl. Acad. Sci. USA 2018 115 E4061 E4070 10.1073/pnas.1712345115 29632181 PMC5924876 · DOI
  81. [86]Schiewer M.J. Goodwin J.F. Han S. Brenner J.C. Augello M.A. Dean J.L. Liu F. Planck J.L. Ravindranathan P. Chinnaiyan A.M. Dual roles of PARP-1 promote cancer growth and progression Cancer Discov. 2012 2 1134 1149 10.1158/2159-8290.CD-12-0120 22993403 PMC3519969 · DOI
  82. [87]Schiewer M.J. Mandigo A.C. Gordon N. Huang F. Gaur S. de Leeuw R. Zhao S.G. Evans J. Han S. Parsons T. PARP-1 regulates DNA repair factor availability EMBO Mol. Med. 2018 10 e8816 10.15252/emmm.201708816 30467127 PMC6284389 · DOI
  83. [88]Chini E.N. CD38 as a regulator of cellular NAD: A novel potential pharmacological target for metabolic conditions Curr. Pharm. Des. 2009 15 57 63 10.2174/138161209787185788 19149603 PMC2883294 · DOI
  84. [89]Camacho-Pereira J. Tarrago M.G. Chini C.C.S. Nin V. Escande C. Warner G.M. Puranik A.S. Schoon R.A. Reid J.M. Galina A. CD38 Dictates Age-Related NAD Decline and Mitochondrial Dysfunction through an SIRT3-Dependent Mechanism Cell Metab. 2016 23 1127 1139 10.1016/j.cmet.2016.05.006 27304511 PMC4911708 · DOI · Paper page
  85. [90]Zhao Y.J. Lam C.M. Lee H.C. The membrane-bound enzyme CD38 exists in two opposing orientations Sci. Signal. 2012 5 ra67 10.1126/scisignal.2002700 22969159 · DOI
  86. [91]Malavasi F. Deaglio S. Damle R. Cutrona G. Ferrarini M. Chiorazzi N. CD38 and chronic lymphocytic leukemia: A decade later Blood 2011 118 3470 3478 10.1182/blood-2011-06-275610 21765022 PMC3574275 · DOI
  87. [92]Chini C.C. Guerrico A.M. Nin V. Camacho-Pereira J. Escande C. Barbosa M.T. Chini E.N. Targeting of NAD metabolism in pancreatic cancer cells: Potential novel therapy for pancreatic tumors Clin. Cancer Res. 2014 20 120 130 10.1158/1078-0432.CCR-13-0150 24025713 PMC3947324 · DOI
  88. [94]Sadej R. Skladanowski A.C. Dual, enzymatic and non-enzymatic, function of ecto-5′-nucleotidase (eN, CD73) in migration and invasion of A375 melanoma cells Acta Biochim. Pol. 2012 59 647 652 23162807
  89. [95]Cerna D. Li H. Flaherty S. Takebe N. Coleman C.N. Yoo S.S. Inhibition of nicotinamide phosphoribosyltransferase (NAMPT) activity by small molecule GMX1778 regulates reactive oxygen species (ROS)-mediated cytotoxicity in a p53- and nicotinic acid phosphoribosyltransferase1 (NAPRT1)-dependent manner J. Biol. Chem. 2012 287 22408 22417 10.1074/jbc.M112.357301 22570471 PMC3381200 · DOI
  90. [96]Audrito V. Messana V.G. Deaglio S. NAMPT and NAPRT: Two Metabolic Enzymes with Key Roles in Inflammation Front. Oncol. 2020 10 358 10.3389/fonc.2020.00358 32266141 PMC7096376 · DOI
  91. [98]Peterse E.F.P. van den Akker B. Niessen B. Oosting J. Suijker J. de Jong Y. Danen E.H.J. Cleton-Jansen A.M. Bovee J. NAD Synthesis Pathway Interference Is a Viable Therapeutic Strategy for Chondrosarcoma Mol. Cancer Res. 2017 15 1714 1721 10.1158/1541-7786.MCR-17-0293 28860121 · DOI
  92. [99]Lee J. Kim H. Lee J.E. Shin S.J. Oh S. Kwon G. Kim H. Choi Y.Y. White M.A. Paik S. Selective Cytotoxicity of the NAMPT Inhibitor FK866 toward Gastric Cancer Cells with Markers of the Epithelial-Mesenchymal Transition, Due to Loss of NAPRT Gastroenterology 2018 155 799 814.e13 10.1053/j.gastro.2018.05.024 29775598 · DOI
  93. [100]Li X.Q. Lei J. Mao L.H. Wang Q.L. Xu F. Ran T. Zhou Z.H. He S. NAMPT and NAPRT, Key Enzymes in NAD Salvage Synthesis Pathway, Are of Negative Prognostic Value in Colorectal Cancer Front. Oncol. 2019 9 736 10.3389/fonc.2019.00736 31448236 PMC6691178 · DOI
  94. [101]Duarte-Pereira S. Pereira-Castro I. Silva S.S. Correia M.G. Neto C. da Costa L.T. Amorim A. Silva R.M. Extensive regulation of nicotinate phosphoribosyltransferase (NAPRT) expression in human tissues and tumors Oncotarget 2016 7 1973 1983 10.18632/oncotarget.6538 26675378 PMC4811510 · DOI
  95. [102]Chowdhry S. Zanca C. Rajkumar U. Koga T. Diao Y. Raviram R. Liu F. Turner K. Yang H. Brunk E. NAD metabolic dependency in cancer is shaped by gene amplification and enhancer remodelling Nature 2019 569 570 575 10.1038/s41586-019-1150-2 31019297 PMC7138021 · DOI
  96. [103]Tateishi K. Wakimoto H. Iafrate A.J. Tanaka S. Loebel F. Lelic N. Wiederschain D. Bedel O. Deng G. Zhang B. Extreme Vulnerability of IDH1 Mutant Cancers to NAD+ Depletion Cancer Cell 2015 28 773 784 10.1016/j.ccell.2015.11.006 26678339 PMC4684594 · DOI · Paper page
  97. [104]Pramono A.A. Rather G.M. Herman H. Lestari K. Bertino J.R. NAD- and NADPH-Contributing Enzymes as Therapeutic Targets in Cancer: An Overview Biomolecules 2020 10 358 10.3390/biom10030358 PMC7175141 32111066 · DOI
  98. [105]Fons N.R. Sundaram R.K. Breuer G.A. Peng S. McLean R.L. Kalathil A.N. Schmidt M.S. Carvalho D.M. Mackay A. Jones C. PPM1D mutations silence NAPRT gene expression and confer NAMPT inhibitor sensitivity in glioma Nat. Commun. 2019 10 3790 10.1038/s41467-019-11732-6 31439867 PMC6706443 · DOI
  99. [106]Piacente F. Caffa I. Ravera S. Sociali G. Passalacqua M. Vellone V.G. Becherini P. Reverberi D. Monacelli F. Ballestrero A. Nicotinic Acid Phosphoribosyltransferase Regulates Cancer Cell Metabolism, Susceptibility to NAMPT Inhibitors, and DNA Repair Cancer Res. 2017 77 3857 3869 10.1158/0008-5472.CAN-16-3079 28507103 · DOI · Paper page
  100. [108]Ghanem M.S. Monacelli F. Nencioni A. Advances in NAD-Lowering Agents for Cancer Treatment Nutrients 2021 13 1665 10.3390/nu13051665 34068917 PMC8156468 · DOI
  101. [109]Gaut Z.N. Solomon H.M. Uptake and metabolism of nicotinic acid by human blood platelets. Effects of structure analogs and metabolic inhibitors Biochim. Biophys. Acta 1970 201 316 322 10.1016/0304-4165(70)90306-5 4313943 · DOI
  102. [110]Carnero A. Lleonart M. The hypoxic microenvironment: A determinant of cancer stem cell evolution Bioessays 2016 38 (Suppl. S1) S65 S74 10.1002/bies.201670911 27417124 · DOI
  103. [111]Peiris-Pages M. Martinez-Outschoorn U.E. Pestell R.G. Sotgia F. Lisanti M.P. Cancer stem cell metabolism Breast Cancer Res. 2016 18 55 10.1186/s13058-016-0712-6 27220421 PMC4879746 · DOI · Paper page
  104. [112]Bao B. Ahmad A. Azmi A.S. Ali S. Sarkar F.H. Overview of cancer stem cells (CSCs) and mechanisms of their regulation: Implications for cancer therapy Curr. Protoc. Pharmacol. 2013 14 25 10.1002/0471141755.ph1425s61 23744710 PMC3733496 · DOI
  105. [113]Espinosa-Sanchez A. Suarez-Martinez E. Sanchez-Diaz L. Carnero A. Therapeutic Targeting of Signaling Pathways Related to Cancer Stemness Front. Oncol. 2020 10 1533 10.3389/fonc.2020.01533 32984007 PMC7479251 · DOI
  106. [114]Korotchkina L. Kazyulkin D. Komarov P.G. Polinsky A. Andrianova E.L. Joshi S. Gupta M. Vujcic S. Kononov E. Toshkov I. OT-82, a novel anticancer drug candidate that targets the strong dependence of hematological malignancies on NAD biosynthesis Leukemia 2020 34 1828 1839 10.1038/s41375-019-0692-5 31896781 PMC7326709 · DOI
  107. [115]Takahashi K. Yamanaka S. Induction of pluripotent stem cells from mouse embryonic and adult fibroblast cultures by defined factors Cell 2006 126 663 676 10.1016/j.cell.2006.07.024 16904174 · DOI · Paper page
  108. [116]Fessler E. Dijkgraaf F.E. De Sousa E.M.F. Medema J.P. Cancer stem cell dynamics in tumor progression and metastasis: Is the microenvironment to blame? Cancer Lett. 2013 341 97 104 10.1016/j.canlet.2012.10.015 23089245 · DOI
  109. [117]Snyder V. Reed-Newman T.C. Arnold L. Thomas S.M. Anant S. Cancer Stem Cell Metabolism and Potential Therapeutic Targets Front. Oncol. 2018 8 203 10.3389/fonc.2018.00203 29922594 PMC5996058 · DOI
  110. [118]Teslaa T. Teitell M.A. Pluripotent stem cell energy metabolism: An update EMBO J. 2015 34 138 153 10.15252/embj.201490446 25476451 PMC4337063 · DOI
  111. [119]Sancho P. Barneda D. Heeschen C. Hallmarks of cancer stem cell metabolism Br. J. Cancer 2016 114 1305 1312 10.1038/bjc.2016.152 27219018 PMC4984474 · DOI
  112. [120]Deshmukh A. Deshpande K. Arfuso F. Newsholme P. Dharmarajan A. Cancer stem cell metabolism: A potential target for cancer therapy Mol. Cancer 2016 15 69 10.1186/s12943-016-0555-x 27825361 PMC5101698 · DOI
  113. [121]Karsten U. Goletz S. What makes cancer stem cell markers different? Springerplus 2013 2 301 10.1186/2193-1801-2-301 23888272 PMC3710573 · DOI
  114. [122]Son M.J. Son M.Y. Seol B. Kim M.J. Yoo C.H. Han M.K. Cho Y.S. Nicotinamide overcomes pluripotency deficits and reprogramming barriers Stem Cells 2013 31 1121 1135 10.1002/stem.1368 23526681 · DOI
  115. [123]Yuan Y. Yan Z. Miao J. Cai R. Zhang M. Wang Y. Wang L. Dang W. Wang D. Xiang D. Autofluorescence of NADH is a new biomarker for sorting and characterizing cancer stem cells in human glioma Stem Cell Res. Ther. 2019 10 330 10.1186/s13287-019-1467-7 31747975 PMC6865050 · DOI
  116. [124]Bonuccelli G. De Francesco E.M. de Boer R. Tanowitz H.B. Lisanti M.P. NADH autofluorescence, a new metabolic biomarker for cancer stem cells: Identification of Vitamin C and CAPE as natural products targeting “stemness” Oncotarget 2017 8 20667 20678 10.18632/oncotarget.15400 28223550 PMC5400535 · DOI
  117. [125]Cui Q. Wang J.Q. Assaraf Y.G. Ren L. Gupta P. Wei L. Ashby C.R. Jr. Yang D.H. Chen Z.S. Modulating ROS to overcome multidrug resistance in cancer Drug Resist. Updat. 2018 41 1 25 10.1016/j.drup.2018.11.001 30471641 · DOI
  118. [126]Panieri E. Santoro M.M. ROS homeostasis and metabolism: A dangerous liason in cancer cells Cell Death Dis. 2016 7 e2253 10.1038/cddis.2016.105 27277675 PMC5143371 · DOI
  119. [127]Von Heideman A. Berglund A. Larsson R. Nygren P. Safety and efficacy of NAD depleting cancer drugs: Results of a phase I clinical trial of CHS 828 and overview of published data Cancer Chemother. Pharmacol. 2010 65 1165 1172 10.1007/s00280-009-1125-3 19789873 · DOI · Paper page
  120. [128]Skelton L.A. Ormerod M.G. Titley J.C. Jackman A.L. Cell cycle effects of CB30865, a lipophilic quinazoline-based analogue of the antifolate thymidylate synthase inhibitor ICI 198583 with an undefined mechanism of action Cytometry 1998 33 56 66 10.1002/(SICI)1097-0320(19980901)33:1<56::AID-CYTO7>3.0.CO;2-9 9725559 · DOI
  121. [129]Fleischer T.C. Murphy B.R. Flick J.S. Terry-Lorenzo R.T. Gao Z.H. Davis T. McKinnon R. Ostanin K. Willardsen J.A. Boniface J.J. Chemical proteomics identifies Nampt as the target of CB30865, an orphan cytotoxic compound Chem. Biol. 2010 17 659 664 10.1016/j.chembiol.2010.05.008 20609415 · DOI
  122. [130]Bavetsias V. Skelton L.A. Yafai F. Mitchell F. Wilson S.C. Allan B. Jackman A.L. The design and synthesis of water-soluble analogues of CB30865, a quinazolin-4-one-based antitumor agent J. Med. Chem. 2002 45 3692 3702 10.1021/jm011081s 12166942 · DOI
  123. [131]O’Brien T. Oeh J. Xiao Y. Liang X. Vanderbilt A. Qin A. Yang L. Lee L.B. Ly J. Cosino E. Supplementation of nicotinic acid with NAMPT inhibitors results in loss of in vivo efficacy in NAPRT1-deficient tumor models Neoplasia 2013 15 1314 1329 10.1593/neo.131718 24403854 PMC3884523 · DOI
  124. [132]Xiao Y. Elkins K. Durieux J.K. Lee L. Oeh J. Yang L.X. Liang X. DelNagro C. Tremayne J. Kwong M. Dependence of tumor cell lines and patient-derived tumors on the NAD salvage pathway renders them sensitive to NAMPT inhibition with GNE-618 Neoplasia 2013 15 1151 1160 10.1593/neo.131304 24204194 PMC3819631 · DOI
  125. [133]Zabka T.S. Singh J. Dhawan P. Liederer B.M. Oeh J. Kauss M.A. Xiao Y. Zak M. Lin T. McCray B. Retinal toxicity, in vivo and in vitro, associated with inhibition of nicotinamide phosphoribosyltransferase Toxicol. Sci. 2015 144 163 172 10.1093/toxsci/kfu268 25505128 · DOI
  126. [134]Baichwal V.R. Willardsen J.A. Lockman J.W. Murphy B.R. Gordillo R. Fleischer T.C. Bradford C. Papac D.I. Mather G.G. Carlson R.O. Activity of the cancer metabolism inhibitor MPC-9528 in xenograft models: Comparison of different dosing schedules J. Clin. Oncol. 2011 29 10529 10.1200/jco.2011.29.15_suppl.10529 · DOI
  127. [135]Matheny C.J. Wei M.C. Bassik M.C. Donnelly A.J. Kampmann M. Iwasaki M. Piloto O. Solow-Cordero D.E. Bouley D.M. Rau R. Next-generation NAMPT inhibitors identified by sequential high-throughput phenotypic chemical and functional genomic screens Chem. Biol. 2013 20 1352 1363 10.1016/j.chembiol.2013.09.014 24183972 PMC3881547 · DOI
  128. [136]Olesen U.H. Petersen J.G. Garten A. Kiess W. Yoshino J. Imai S. Christensen M.K. Fristrup P. Thougaard A.V. Bjorkling F. Target enzyme mutations are the molecular basis for resistance towards pharmacological inhibition of nicotinamide phosphoribosyltransferase BMC Cancer 2010 10 677 10.1186/1471-2407-10-677 21144000 PMC3019212 · DOI
  129. [137]Zhao G. Green C.F. Hui Y.H. Prieto L. Shepard R. Dong S. Wang T. Tan B. Gong X. Kays L. Discovery of a Highly Selective NAMPT Inhibitor That Demonstrates Robust Efficacy and Improved Retinal Toxicity with Nicotinic Acid Coadministration Mol. Cancer Ther. 2017 16 2677 2688 10.1158/1535-7163.MCT-16-0674 29054982 · DOI
  130. [138]Estoppey D. Hewett J.W. Guy C.T. Harrington E. Thomas J.R. Schirle M. Cuttat R. Waldt A. Gerrits B. Yang Z. Identification of a novel NAMPT inhibitor by CRISPR/Cas9 chemogenomic profiling in mammalian cells Sci. Rep. 2017 7 42728 10.1038/srep42728 28205648 PMC5311948 · DOI
  131. [139]Esposito E. Impellizzeri D. Mazzon E. Fakhfouri G. Rahimian R. Travelli C. Tron G.C. Genazzani A.A. Cuzzocrea S. The NAMPT inhibitor FK866 reverts the damage in spinal cord injury J. Neuroinflammation 2012 9 66 10.1186/1742-2094-9-66 22490786 PMC3353188 · DOI
  132. [140]Bai J. Liao C. Liu Y. Qin X. Chen J. Qiu Y. Qin D. Li Z. Tu Z.C. Jiang S. Structure-Based Design of Potent Nicotinamide Phosphoribosyltransferase Inhibitors with Promising In Vitro and In Vivo Antitumor Activities J. Med. Chem. 2016 59 5766 5779 10.1021/acs.jmedchem.6b00324 27224875 · DOI
  133. [141]Travelli C. Aprile S. Mattoteia D. Colombo G. Clemente N. Scanziani E. Terrazzino S. Alisi M.A. Polenzani L. Grosa G. Identification of potent triazolylpyridine nicotinamide phosphoribosyltransferase (NAMPT) inhibitors bearing a 1,2,3-triazole tail group Eur. J. Med. Chem. 2019 181 111576 10.1016/j.ejmech.2019.111576 31400709 · DOI
  134. [142]Zhang K. Ni Y. Chen J. Tu Z. Wu X. Chen D. Yao H. Jiang S. Discovery of trans-3-(pyridin-3-yl)acrylamide-derived sulfamides as potent nicotinamide phosphoribosyltransferase (NAMPT) inhibitors for the potential treatment of cancer Bioorg. Med. Chem. Lett. 2019 29 1502 1506 10.1016/j.bmcl.2019.04.013 30992165 · DOI
  135. [143]Wilsbacher J.L. Cheng M. Cheng D. Trammell S.A.J. Shi Y. Guo J. Koeniger S.L. Kovar P.J. He Y. Selvaraju S. Discovery and Characterization of Novel Nonsubstrate and Substrate NAMPT Inhibitors Mol. Cancer Ther. 2017 16 1236 1245 10.1158/1535-7163.MCT-16-0819 28468779 · DOI
  136. [144]Mudd S.R. Voorbach M.J. Cheng D. Cheng M. Guo J. Gao W. Buchanan F.G. Tse C. Wilsbacher J. Utilization of (18)F-Fluorodeoxyglucose-Positron Emission Tomography to Understand the Mechanism of Nicotinamide Phosphoribosyltransferase Inhibitors In Vivo J. Pharmacol. Exp. Ther. 2019 371 583 589 10.1124/jpet.119.259135 31562200 · DOI
  137. [145]Zhang S.L. Xu T.Y. Yang Z.L. Han S. Zhao Q. Miao C.Y. Crystal structure-based comparison of two NAMPT inhibitors Acta Pharmacol. Sin. 2018 39 294 301 10.1038/aps.2017.80 28858298 PMC5800471 · DOI
  138. [146]Xu T.Y. Zhang S.L. Dong G.Q. Liu X.Z. Wang X. Lv X.Q. Qian Q.J. Zhang R.Y. Sheng C.Q. Miao C.Y. Discovery and characterization of novel small-molecule inhibitors targeting nicotinamide phosphoribosyltransferase Sci. Rep. 2015 5 10043 10.1038/srep10043 26040985 PMC4603696 · DOI
  139. [147]Kraus D. Reckenbeil J. Veit N. Kuerpig S. Meisenheimer M. Beier I. Stark H. Winter J. Probstmeier R. Targeting glucose transport and the NAD pathway in tumor cells with STF-31: A re-evaluation Cell Oncol. 2018 41 485 494 10.1007/s13402-018-0385-5 PMC12995222 29949049 · DOI
  140. [148]Dong G. Chen W. Wang X. Yang X. Xu T. Wang P. Zhang W. Rao Y. Miao C. Sheng C. Small Molecule Inhibitors Simultaneously Targeting Cancer Metabolism and Epigenetics: Discovery of Novel Nicotinamide Phosphoribosyltransferase (NAMPT) and Histone Deacetylase (HDAC) Dual Inhibitors J. Med. Chem. 2017 60 7965 7983 10.1021/acs.jmedchem.7b00467 28885834 · DOI
  141. [149]Palacios D.S. Meredith E.L. Kawanami T. Adams C.M. Chen X. Darsigny V. Palermo M. Baird D. George E.L. Guy C. Scaffold Morphing Identifies 3-Pyridyl Azetidine Ureas as Inhibitors of Nicotinamide Phosphoribosyltransferase (NAMPT) ACS Med. Chem. Lett. 2019 10 1524 1529 10.1021/acsmedchemlett.9b00325 31749905 PMC6862340 · DOI
  142. [150]Karpov A.S. Abrams T. Clark S. Raikar A. D’Alessio J.A. Dillon M.P. Gesner T.G. Jones D. Lacaud M. Mallet W. Nicotinamide Phosphoribosyltransferase Inhibitor as a Novel Payload for Antibody-Drug Conjugates ACS Med. Chem. Lett. 2018 9 838 842 10.1021/acsmedchemlett.8b00254 30128077 PMC6088352 · DOI
  143. [151]Neumann C.S. Olivas K.C. Anderson M.E. Cochran J.H. Jin S. Li F. Loftus L.V. Meyer D.W. Neale J. Nix J.C. Targeted Delivery of Cytotoxic NAMPT Inhibitors Using Antibody-Drug Conjugates Mol. Cancer Ther. 2018 17 2633 2642 10.1158/1535-7163.MCT-18-0643 30242091 · DOI
  144. [152]Lameijer L.N. Ernst D. Hopkins S.L. Meijer M.S. Askes S.H.C. Le Dévédec S.E. Bonnet S. A Red-Light-Activated Ruthenium-Caged NAMPT Inhibitor Remains Phototoxic in Hypoxic Cancer Cells Angew. Chem. 2017 56 11549 11553 10.1002/anie.201703890 28666065 PMC5601216 · DOI
  145. [153]Heske C.M. Davis M.I. Baumgart J.T. Wilson K. Gormally M.V. Chen L. Zhang X. Ceribelli M. Duveau D.Y. Guha R. Matrix Screen Identifies Synergistic Combination of PARP Inhibitors and Nicotinamide Phosphoribosyltransferase (NAMPT) Inhibitors in Ewing Sarcoma Clin. Cancer Res. 2017 23 7301 7311 10.1158/1078-0432.CCR-17-1121 28899971 PMC6636827 · DOI
  146. [154]Galli U. Colombo G. Travelli C. Tron G.C. Genazzani A.A. Grolla A.A. Recent Advances in NAMPT Inhibitors: A Novel Immunotherapic Strategy Front. Pharmacol. 2020 11 656 10.3389/fphar.2020.00656 32477131 PMC7235340 · DOI · Paper page
  147. [155]Aprile S. Galli U. Tron G.C. Del Grosso E. Travelli C. Grosa G. Data on metabolic stability, aqueous solubility and CYP inhibition of novel triazole-based nicotinamide phosphoribosyltransferase (NAMPT) inhibitors Data Brief. 2020 28 105034 10.1016/j.dib.2019.105034 32226807 PMC7093798 · DOI
  148. [156]Adams D.J. Ito D. Rees M.G. Seashore-Ludlow B. Puyang X. Ramos A.H. Cheah J.H. Clemons P.A. Warmuth M. Zhu P. NAMPT is the cellular target of STF-31-like small-molecule probes ACS Chem. Biol. 2014 9 2247 2254 10.1021/cb500347p 25058389 PMC4201331 · DOI
  149. [157]Abu Aboud O. Chen C.H. Senapedis W. Baloglu E. Argueta C. Weiss R.H. Dual and Specific Inhibition of NAMPT and PAK4 By KPT-9274 Decreases Kidney Cancer Growth Mol. Cancer Ther. 2016 15 2119 2129 10.1158/1535-7163.MCT-16-0197 27390344 PMC5010932 · DOI
  150. [158]Aboukameel A. Muqbil I. Senapedis W. Baloglu E. Landesman Y. Shacham S. Kauffman M. Philip P.A. Mohammad R.M. Azmi A.S. Novel p21-Activated Kinase 4 (PAK4) Allosteric Modulators Overcome Drug Resistance and Stemness in Pancreatic Ductal Adenocarcinoma Mol. Cancer Ther. 2017 16 76 87 10.1158/1535-7163.MCT-16-0205 28062705 PMC5221563 · DOI
  151. [159]Rane C. Senapedis W. Baloglu E. Landesman Y. Crochiere M. Das-Gupta S. Minden A. A novel orally bioavailable compound KPT-9274 inhibits PAK4, and blocks triple negative breast cancer tumor growth Sci. Rep. 2017 7 42555 10.1038/srep42555 28198380 PMC5309789 · DOI
  152. [160]Radu M. Semenova G. Kosoff R. Chernoff J. PAK signalling during the development and progression of cancer Nat. Rev. Cancer 2014 14 13 25 10.1038/nrc3645 24505617 PMC4115244 · DOI
  153. [161]Somers K. Evans K. Cheung L. Karsa M. Pritchard T. Kosciolek A. Bongers A. El-Ayoubi A. Forgham H. Middlemiss S. Effective targeting of NAMPT in patient-derived xenograft models of high-risk pediatric acute lymphoblastic leukemia Leukemia 2020 34 1524 1539 10.1038/s41375-019-0683-6 31848452 PMC9110273 · DOI

Authors
Navas, L. E., & Carnero, A.
Affiliations
Consejo Superior de Investigaciones Científicas (ES)
Corresponding author
Carnero, Amancio
ORCID
Carnero, Amancio
Venue
Cells
Publisher
MDPI AG
Published
2022-08-24
Volume
11
Issue
17
Pages
2627
ISSN
2073-4409 (ISSN-L)
DOI
10.3390/cells11172627
PMC
PMC9454445
OpenAlex
W4293008982
Cited by
68
References
161
Citations by year
2026: 17 · 2025: 26 · 2024: 15 · 2023: 9 · 2022: 1
FWCI
1.82
Type
journal article
Language
en
Open access
Licence
Locations
  • Cells (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • RISalud Institutional Health Repository of Andalucía (submittedVersion, cc-by)
  • DIGITAL.CSIC (Spanish National Research Council (CSIC)) (submittedVersion, cc-by)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
  • Ministerio de Ciencia e Innovación (MCI), Plan Estatal de I+D+I 2021, a la Agencia Estatal de Investigación (AEI) y al Fondo Europeo de Desarrollo Regional (MCI/AEI/FEDER, UE) (RTI2018-097455-B-I00, ID2021-122629OB-I00, GC16173720CARR)
  • FEDER from Regional Development European Funds (European Union) (RTI2018-097455-B-I00, ID2021-122629OB-I00, GC16173720CARR)
  • European Regional Development Fund (ERDF) from the Regional Ministry of Economic Transformation, Industry, Knowledge and Universities (RTI2018-097455-B-I00, ID2021-122629OB-I00, GC16173720CARR)
  • AECC (Spanish Association of Cancer Research) (RTI2018-097455-B-I00, ID2021-122629OB-I00, GC16173720CARR)
  • FPU from Ministerio de Ciencia, Innovación y Universidades (MCIU) Plan Estatal de I+D+I 2016 (RTI2018-097455-B-I00, ID2021-122629OB-I00, GC16173720CARR)
Topics
  • Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Calcium signaling and nucleotide metabolism
Keywords
NAD+ metabolism, visfatin, NAD+ salvage pathway, sirtuins, poly(ADP-ribose) polymerase, cyclic ADP-ribose, ADP-ribosylation, NAMPT inhibitors, cancer therapy targets, tumor cell proliferation, apoptosis, redox metabolism
MeSH terms
Adenosine Diphosphate Ribose, Humans, NAD, Neoplasms, Poly(ADP-ribose) Polymerases, Sirtuins

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