NAD + /NADH and NADP + /NADPH in Cellular Functions and Cell Death: Regulation and Biological Consequences
Abstract
Accumulating evidence has suggested that NAD (including NAD+ and NADH) and NADP (including NADP+ and NADPH) could belong to the fundamental common mediators of various biological processes, including energy metabolism, mitochondrial functions, calcium homeostasis, antioxidation/generation of oxidative stress, gene expression, immunological functions, aging, and cell death: First, it is established that NAD mediates energy metabolism and mitochondrial functions; second, NADPH is a key component in cellular antioxidation systems; and NADH-dependent reactive oxygen species (ROS) generation from mitochondria and NADPH oxidase-dependent ROS generation are two critical mechanisms of ROS generation; third, cyclic ADP-ribose and several other molecules that are generated from NAD and NADP could mediate calcium homeostasis; fourth, NAD and NADP modulate multiple key factors in cell death, such as mitochondrial permeability transition, energy state, poly(ADP-ribose) polymerase-1, and apoptosis-inducing factor; and fifth, NAD and NADP profoundly affect aging-influencing factors such as oxidative stress and mitochondrial activities, and NAD-dependent sirtuins also mediate the aging process. Moreover, many recent studies have suggested novel paradigms of NAD and NADP metabolism. Future investigation into the metabolism and biological functions of NAD and NADP may expose fundamental properties of life, and suggest new strategies for treating diseases and slowing the aging process.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
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?
Alternatively, substrate flow through the TCA cycle differs depending on substrates, which might affect the activity of NADP+-dependent isocitrate dehydrogenase and malic enzyme.
“Alternatively, the substrate flow through the TCA cycle differs depending on the substrates, which might affect the activity of the other two mitochondrial NADPH-regenerating enzymes the NADP + -dependent isocitrate dehydrogenase [119,120] and the malic enzyme [118,121].”
From Differential effects of complex II on mitochondrial ROS production and their relation to cardioprotective pre- and postconditioning (2013) · cites this paper as [121]
The NAD+/NADH ratio is important in bioenergetic reactions across subcellular compartments, and increased activity of one reaction can alter metabolic homeostasis via changes in this ratio.
“The ratio of NAD+/NADH is important in various bioenergetic reactions in different subcellular compartments, and increased activity of one of these reactions can influence the metabolic homeostasis via changes in the NAD+/NADH ratio (Ying, 2008).”
From NAD+ in Brain Aging and Neurodegenerative Disorders (2019) · cites this paper as Ying, 2008
Conversion of NAD+ to NADP+/NADPH is important for antioxidation, oxidative stress generation, calcium homeostasis, and cell survival or death.
“Additionally, the conversion of NAD+ to NADP+/NADPH is important in the involvement of different cellular functions, including antioxidation and generation of oxidative stress, calcium homeostasis, and cell survival or death (Ying, 2008).”
From NAD+ in Brain Aging and Neurodegenerative Disorders (2019) · cites this paper as Ying, 2008
Superoxide from mitochondrial electron transport and NADPH oxidase are the two major routes of cellular ROS production, and NAD+/NADH and NADP+/NADPH play key roles in cellular antioxidant systems.
“Superoxide produced during mitochondrial electron transport and via the activity of NADPH oxidase are the two major routes of cellular ROS production, and both NAD+/NADH and NADP+/NADPH play key roles in cellular antioxidant systems (Ying, 2008).”
From NAD+ in Brain Aging and Neurodegenerative Disorders (2019) · cites this paper as Ying, 2008
Cites
1 retracted
Visfatin: A Protein Secreted by Visceral Fat That Mimics the Effects of Insulin
Fukuhara, A., Matsuda, M., Nishizawa, M., Segawa, K., Tanaka, M., Kishimoto, K., Matsuki, Y., Murakami, M., Ichisaka, T., Murakami, H., et al. (2005) · Science · doi:10.1126/science.1097243 · Cited by 1,906 · see citing works
RetractedFree radicals and antioxidants in normal physiological functions and human disease
Valko, M., Leibfritz, D., Moncol, J., Cronin, M. T. D., Mazur, M., & Telser, J. (2007) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2006.07.001 · Cited by 14,269 · see citing works
Green, D. R., & Reed, J. C. (1998) · Science · doi:10.1126/science.281.5381.1309 · Cited by 8,998 · see citing works
The NOX Family of ROS-Generating NADPH Oxidases: Physiology and Pathophysiology
Bedard, K., & Krause, K.-H. (2007) · Physiological Reviews · doi:10.1152/physrev.00044.2005 · Cited by 6,989 · see citing works
Glutathione Metabolism and Its Implications for Health
Wu, G., Lupton, J. R., Turner, N. D., Fang, Y.-Z., & Yang, S. (2004) · The Journal of Nutrition · doi:10.1093/jn/134.3.489 · Cited by 3,842 · 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
Mitochondrial free radical generation, oxidative stress, and aging
Cadenas, E., & Davies, K. J. A. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00317-8 · Cited by 3,010 · 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
Physiological functions of thioredoxin and thioredoxin reductase
Arnér, E. S. J., & Holmgren, A. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01701.x · Cited by 2,535 · see citing works
The mitochondrial permeability transition
Zoratti, M., & Szabó, I. (1995) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/0304-4157(95)00003-a · Cited by 2,395 · see citing works
Negative Control of p53 by Sir2α Promotes Cell Survival under Stress
Luo, J., Nikolaev, A. Y., Imai, S.-I., Chen, D., Su, F., Shiloh, A., Guarente, L., & Gu, W. (2001) · Cell · doi:10.1016/s0092-8674(01)00524-4 · Cited by 2,081 · see citing works
Oxidative damage and mitochondrial decay in aging.
Shigenaga, M. K., Hagen, T. M., & Ames, B. N. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.23.10771 · Cited by 2,055 · see citing works
Antioxidant and redox regulation of gene transcription
Sen, C. K., & Packer, L. (1996) · The FASEB Journal · doi:10.1096/fasebj.10.7.8635688 · Cited by 1,996 · see citing works
Poly(ADP-ribose): novel functions for an old molecule
Schreiber, V., Dantzer, F., Amé, J., & de MURCIA, G. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1963 · Cited by 1,917 · see citing works
Mediation of Poly(ADP-Ribose) Polymerase-1-Dependent Cell Death by Apoptosis-Inducing Factor
Yu, S.-W., Wang, H., Poitras, M. F., Coombs, C., Bowers, W. J., Federoff, H. J., Poirier, G. G., Dawson, T. M., & Dawson, V. L. (2002) · Science · doi:10.1126/science.1072221 · Cited by 1,826 · see citing works
Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions
D’Amours, D., Desnoyers, S., D’Silva, I., & Poirier, G. G. (1999) · Biochemical Journal · doi:10.1042/bj3420249 · Cited by 1,819 · see citing works
Sirtuins in mammals: insights into their biological function
Michán, S., & Sinclair, D. A. (2007) · Biochemical Journal · doi:10.1042/bj20070140 · Cited by 1,719 · see citing works
Telomeres and human disease: ageing, cancer and beyond
Blasco, M. A. (2005) · Nature Reviews Genetics · doi:10.1038/nrg1656 · Cited by 1,690 · see citing works
Genomic Instability and Aging-like Phenotype in the Absence of Mammalian SIRT6
Mostoslavsky, R., Chua, K. F., Lombard, D. B., Pang, W. W., Fischer, M. R., Gellon, L., Liu, P., Mostoslavsky, G., Franco, S., Murphy, M. M., et al. (2006) · Cell · doi:10.1016/j.cell.2005.11.044 · Cited by 1,637 · see citing works
Reactive Oxygen Radicals in Signaling and Damage in the Ischemic Brain
Chan, P. H. (2001) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1097/00004647-200101000-00002 · Cited by 1,589 · see citing works
The Sir2 Family of Protein Deacetylases
Blander, G., & Guarente, L. (2004) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.073651 · Cited by 1,496 · see citing works
Mitochondrial control of apoptosis
Kroemer, G., Zamzami, N., & Susín, S. A. (1997) · Immunology Today · doi:10.1016/s0167-5699(97)80014-x · Cited by 1,492 · see citing works
Lemasters, J. J., Nieminen, A.-L., Qian, T., Trost, L. C., Elmore, S. P., Nishimura, Y., Crowe, R. A., Cascio, W. E., Bradham, C. A., Brenner, D. A., et al. (1998) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(98)00112-1 · Cited by 1,387 · see citing works
The Therapeutic Potential of Poly(ADP-Ribose) Polymerase Inhibitors
Virág, L., & Szabó, C. (2002) · Pharmacological Reviews · doi:10.1124/pr.54.3.375 · Cited by 1,373 · see citing works
Mammalian SIRT1 Represses Forkhead Transcription Factors
Motta, M. C., Divecha, N., Lemieux, M. E., Kamel, C., Chen, D., Gu, W. J., Bultsma, Y., McBurney, M. W., & Guarente, L. (2004) · Cell · doi:10.1016/s0092-8674(04)00126-6 · Cited by 1,351 · see citing works
Mechanisms of Cell Death in Oxidative Stress
Ryter, S. W., Kim, H. P., Hoetzel, A., Park, J. W., Nakahira, K., Wang, X., & Choi, A. M. K. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.9.49 · Cited by 1,262 · see citing works
Nitric Oxide Activation of Poly(ADP-Ribose) Synthetase in Neurotoxicity
Zhang, J., Dawson, V. L., Dawson, T. M., & Snyder, S. H. (1994) · Science · doi:10.1126/science.8080500 · Cited by 1,118 · see citing works
Nitric oxide and superoxide in inflammation and immune regulation.
Guzik, T. J., Korbut, R., & Adamek-Guzik, T. (2003) · PubMed · Cited by 1,096 · see citing works
S-nitrosylated GAPDH initiates apoptotic cell death by nuclear translocation following Siah1 binding
Hara, M. R., Agrawal, N., Kim, S. F., Cascio, M. B., Fujimuro, M., Ozeki, Y., Takahashi, M., Cheah, J. H., Tankou, S. K., Hester, L. D., et al. (2005) · Nature Cell Biology · doi:10.1038/ncb1268 · Cited by 1,071 · see citing works
Increased Nuclear NAD Biosynthesis and SIRT1 Activation Prevent Axonal Degeneration
Araki, T., Sasaki, Y., & Milbrandt, J. (2004) · Science · doi:10.1126/science.1098014 · Cited by 1,060 · see citing works
Regulation of clock and NPAS2 DNA binding by the redox state of NAD cofactors
Rutter, J., Reick, M., Wu, L. C., & McKnight, S. L. (2001) · Science · doi:10.1126/science.1060698 · Cited by 1,059 · see citing works
Role of Oxidants in Ischemic Brain Damage
Chan, P. H. (1996) · Stroke · doi:10.1161/01.str.27.6.1124 · Cited by 1,027 · see citing works
Cloning and Characterization of the cDNA Encoding a Novel Human pre-B-Cell Colony-enhancing Factor
Samal, B. B., Sun, Y., Stearns, G., Xie, C., Suggs, S. V., & McNiece, I. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.2.1431 · Cited by 1,025 · see citing works
Poly(ADP-ribose) polymerase gene disruption renders mice resistant to cerebral ischemia
Eliasson, M. J. L., Sampei, K., Mandir, A. S., Hurn, P. D., Traystman, R. J., Bao, J., Pieper, A. A., Wang, Z., Dawson, T. M., Snyder, S. H., et al. (1997) · Nature Medicine · doi:10.1038/nm1097-1089 · Cited by 1,019 · see citing works
Revollo, J. R., Grimm, A. A., & Imai, S.-I. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408388200 · Cited by 1,010 · see citing works
NAD+ metabolism in health and disease
Belenky, P. A., Bogan, K. L., & Brenner, C. (2006) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2006.11.006 · Cited by 983 · see citing works
Necrotic death as a cell fatePreprint
Zong, W., & Thompson, C. B. (2006) · Genes & Development · doi:10.1101/gad.1376506 · Cited by 920 · see citing works
Savina, A., Jancic, C. C., Hugues, S., Guermonprez, P., Vargas, P., Moura, I. C., Lennon‐Duménil, A., Seabra, M. C., Raposo, G., & Amigorena, S. (2006) · Cell · doi:10.1016/j.cell.2006.05.035 · Cited by 896 · see citing works
A Topoisomerase IIß-Mediated dsDNA Break Required for Regulated Transcription
Ju, B., Lunyak, V. V., Perissi, V., García-Bassets, I., Rose, D. W., Glass, C. K., & Rosenfeld, M. G. (2006) · Science · doi:10.1126/science.1127196 · Cited by 842 · see citing works
Axon degeneration mechanisms: Commonality amid diversity
Coleman, M. (2005) · Nature reviews. Neuroscience · doi:10.1038/nrn1788 · Cited by 819 · see citing works
Poly(ADP-ribosyl)ation by PARP-1: `PAR-laying' NAD + into a nuclear signalPreprint
Kim, M. Y., Zhang, T., & Kraus, W. L. (2005) · Genes & Development · doi:10.1101/gad.1331805 · Cited by 803 · see citing works
Regulation of Telomerase by Telomeric Proteins
Smogorzewska, A., & de Lange, T. (2004) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.071403.160049 · Cited by 796 · see citing works
Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases
Hallows, W. C., Lee, S., & Denu, J. M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0604392103 · Cited by 792 · see citing works
Mitochondrio‐nuclear translocation of AIF in apoptosis and necrosis
Daugas, É., Susín, S. A., Zamzami, N., Ferri, K. F., Irinopoulou, T., Larochette, N., Prévost, M., Leber, B. F., Andrews, D. W., Penninger, J. M., et al. (2000) · The FASEB Journal · doi:10.1096/fasebj.14.5.729 · Cited by 776 · see citing works
Sauve, A. A., Wolberger, C., Schramm, V. L., & Boeke, J. D. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.74.082803.133500 · Cited by 763 · see citing works
Nicotinamide and PNC1 govern lifespan extension by calorie restriction in Saccharomyces cerevisiae
Anderson, R. M., Bitterman, K. J., Wood, J. G., Medvedik, O., & Sinclair, D. A. (2003) · Nature · doi:10.1038/nature01578 · Cited by 736 · see citing works
The power to reduce: pyridine nucleotides—small molecules with a multitude of functions
Pollak, N., Dölle, C., & Ziegler, M. (2007) · Biochemical Journal · doi:10.1042/bj20061638 · Cited by 730 · see citing works
Apoptosis-inducing factor mediates poly(ADP-ribose) (PAR) polymer-induced cell death
Yu, S.-W., Andrabi, S. A., Wang, H., Kim, N. S., Poirier, G. G., Dawson, T. M., & Dawson, V. L. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0606528103 · Cited by 718 · see citing works
Schwer, B., Bunkenborg, J., Verdin, R. O., Andersen, J. S., & Verdin, E. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0603968103 · Cited by 705 · see citing works
Babior, B. M. (2004) · Current Opinion in Immunology · doi:10.1016/j.coi.2003.12.001 · Cited by 705 · see citing works
Mitochondrial α-Ketoglutarate Dehydrogenase Complex Generates Reactive Oxygen Species
Starkov, A. A., Fiskum, G. M., Chinopoulos, C., Lorenzo, B. J., Browne, S. E., Patel, M. S., & Beal, M. F. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.1899-04.2004 · Cited by 692 · see citing works
Abramov, A. Y., Scorziello, A., & Duchen, M. R. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.4468-06.2007 · Cited by 686 · see citing works
Role of poly(ADP-ribose) synthetase in inflammation and ischaemia–reperfusion
Szabó, C., & Dawson, V. L. (1998) · Trends in Pharmacological Sciences · doi:10.1016/s0165-6147(98)01193-6 · Cited by 685 · see citing works
Di Lisa, F., Menabò, R., Canton, M., Barile, M., & Bernardi, P. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m006825200 · Cited by 678 · see citing works
Tumor Suppressor HIC1 Directly Regulates SIRT1 to Modulate p53-Dependent DNA-Damage Responses
Chen, W., Wang, D. H., Yen, R.-W. C., Luo, J., Gu, W. J., & Baylin, S. B. (2005) · Cell · doi:10.1016/j.cell.2005.08.011 · Cited by 649 · see citing works
Poly(ADP-ribose) (PAR) polymer is a death signal
Andrabi, S. A., Kim, N. S., Yu, S.-W., Wang, H., Koh, D. W., Sasaki, M., Klaus, J. A., Otsuka, T., Zhang, Z., Koehler, R. C., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0606526103 · Cited by 644 · see citing works
Calorie restriction extends yeast life span by lowering the level of NADH
Lin, S.-J., Ford, E., Haigis, M., Liszt, G., & Guarente, L. (2004) · Genes & Development · doi:10.1101/gad.1164804 · Cited by 632 · see citing works
Mammalian Sir2 homolog SIRT7 is an activator of RNA polymerase I transcription
Ford, E., Voit, R., Liszt, G., Magin, C., Grummt, I., & Guarente, L. (2006) · Genes & Development · doi:10.1101/gad.1399706 · Cited by 629 · see citing works
Ischemic Brain Injury is Mediated by the Activation of Poly(ADP-Ribose)Polymerase
Endres, M., Wang, Z., Namura, S., Waeber, C., & Moskowitz, M. A. (1997) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1097/00004647-199711000-00002 · Cited by 622 · see citing works
AIF deficiency compromises oxidative phosphorylation
Vahsen, N., Candé, C., Brière, J.-J., Bénit, P., Joza, N. A., Larochette, N., Mastroberardino, P. G., Péquignot, M. O., Casares, N., Lazar, V., et al. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600461 · Cited by 622 · see citing works
Regulation of Corepressor Function by Nuclear NADH
Zhang, Q., Piston, D. W., & Goodman, R. H. (2002) · Science · doi:10.1126/science.1069300 · Cited by 620 · see citing works
Hasmann, M., & Schemainda, I. (2003) · PubMed · Cited by 618 · see citing works
Alkylating DNA damage stimulates a regulated form of necrotic cell deathPreprint
Zong, W., Ditsworth, D., Bauer, D. E., Wang, Z., & Thompson, C. B. (2004) · Genes & Development · doi:10.1101/gad.1199904 · Cited by 618 · see citing works
Peroxynitrite‐mediated oxidative protein modifications
Ischiropoulos, H., & Al‐Mehdi, A. B. (1995) · FEBS Letters · doi:10.1016/0014-5793(95)00307-u · Cited by 610 · see citing works
Rey, F. E., Cifuentes-Pagano, E., Kiarash, A., Quinn, M. T., & Pagano, P. J. (2001) · Circulation Research · doi:10.1161/hh1701.096037 · Cited by 606 · see citing works
Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions
D’Amours, D., Desnoyers, S., D’Silva, I., & Poirier, G. G. (1999) · Biochemical Journal · doi:10.1042/0264-6021:3420249 · Cited by 600 · see citing works
The thioredoxin system in cancer
Arnér, E. S. J., & Holmgren, A. (2006) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2006.10.009 · Cited by 589 · see citing works
Abramov, A. Y., Canevari, L., & Duchen, M. R. (2004) · The Journal of Neuroscience · doi:10.1523/jneurosci.4042-03.2004 · Cited by 587 · see citing works
Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine
Starai, V. J., Celic, I., Cole, R. N., Boeke, J. D., & Escalante-Semerena, J. C. (2002) · Science · doi:10.1126/science.1077650 · Cited by 564 · see citing works
The redox state of free nicotinamide-adenine dinucleotide phosphate in the cytoplasm of rat liver
Veech, R. L., Eggleston, L. V., & Krebs, H. A. (1969) · Biochemical Journal · doi:10.1042/bj1150609a · Cited by 563 · see citing works
Manipulation of Brain Kynurenines: Glial Targets, Neuronal Effects, and Clinical Opportunities
Schwarcz, R. M., & Pellicciari, R. (2002) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.102.034439 · Cited by 556 · see citing works
Kletzien, R. F., Harris, P. K. W., & Foellmi, L. A. (1994) · The FASEB Journal · doi:10.1096/fasebj.8.2.8119488 · Cited by 551 · see citing works
Kim, M. Y., Mauro, S. A., Gévry, N. Y., Lis, J. T., & Kraus, W. L. (2004) · Cell · doi:10.1016/j.cell.2004.11.002 · Cited by 551 · see citing works
Pandolfi, P. P., Sonati, F., Rivi, R., Mason, P. J., Grosveld, F. G., & Luzzatto, L. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb00205.x · Cited by 547 · see citing works
Jo, S.-H., Son, M.-K., Koh, H.-J., Lee, S.-M., Song, I.-H., Kim, Y.-O., Lee, Y.-S., Jeong, K.-S., Kim, W. B., Park, J.-W., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010120200 · Cited by 536 · see citing works
Poly (ADP-ribose) polymerase, nitric oxide and cell death
Pieper, A. A. (1999) · Trends in Pharmacological Sciences · doi:10.1016/s0165-6147(99)01292-4 · Cited by 521 · see citing works
Poly(ADP-ribosyl)ation of polynucleosomes causes relaxation of chromatin structure.
Poirier, G. G., de MURCIA, G., Jongstra‐Bilen, J., Niedergang, C., & Mandel, P. (1982) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.79.11.3423 · Cited by 516 · see citing works
Berger, F., Lau, C., Dahlmann, M., & Ziegler, M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508660200 · Cited by 508 · see citing works
Redox signaling in angiogenesis: Role of NADPH oxidase
Ushio‐Fukai, M. (2006) · Cardiovascular Research · doi:10.1016/j.cardiores.2006.04.015 · Cited by 489 · see citing works
The new life of a centenarian: signalling functions of NAD(P)
Berger, F. (2004) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2004.01.007 · Cited by 489 · see citing works
Catalase: a tetrameric enzyme with four tightly bound molecules of NADPH.
Kirkman, H., & Gaetani, G. F. (1984) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.81.14.4343 · Cited by 476 · see citing works
Avalos, J. L., Bever, K. M., & Wolberger, C. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.02.022 · Cited by 462 · see citing works
Gill, P. S., & Wilcox, C. S. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.1597 · Cited by 461 · 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
A genetic and physiological study of impaired glucose homeostasis control in C57BL/6J mice
Toye, A. A., Lippiat, J. D., Proks, P., Shimomura, K., Bentley, L., Hugill, A., Mijat, V., Goldsworthy, M. E., Moir, L., Haynes, A. R., et al. (2005) · Diabetologia · doi:10.1007/s00125-005-1680-z · Cited by 438 · see citing works
Physiological functions of cyclic ADP-ribose and NAADP as calcium messengers
Lee, H. C. (2001) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.41.1.317 · Cited by 433 · see citing works
Cytosolic NADP+-dependent isocitrate dehydrogenase status modulates oxidative damage to cells
Lee, S. M., Koh, H., Park, D., Song, B. J., Huh, T., & Park, J. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00815-8 · Cited by 422 · see citing works
PHOSPHORYLATION COUPLED TO OXIDATION OF DIHYDRODIPHOSPHOPYRIDINE NUCLEOTIDE
Lehninger, A. L. (1951) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)56077-4 · Cited by 421 · see citing works
North, R. A., & Barnard, E. A. (1997) · Current Opinion in Neurobiology · doi:10.1016/s0959-4388(97)80062-1 · Cited by 414 · see citing works
Belenky, P., Racette, F. G., Bogan, K. L., McClure, J. M., Smith, J. S., & Brenner, C. (2007) · Cell · doi:10.1016/j.cell.2007.03.024 · Cited by 411 · see citing works
Pillai, J. B., Isbatan, A., Imai, S., & Gupta, M. P. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506162200 · Cited by 391 · see citing works
Oxidative stress signalling in Alzheimer's disease
Zhu, X., Raina, A. K., Lee, H., Casadesús, G., Smith, M. A., & Perry, G. L. (2004) · Brain Research · doi:10.1016/j.brainres.2004.01.012 · Cited by 390 · see citing works
Mandir, A. S., Przedborski, S., Jackson-Lewis, V., Wang, Z.-Q., Simbulan-Rosenthal, C. M., Smulson, M. E., Hoffman, B. E., Guastella, D. B., Dawson, V. L., & Dawson, T. M. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.10.5774 · Cited by 382 · see citing works
Alano, C. C., Ying, W., & Swanson, R. A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313329200 · Cited by 374 · see citing works
Self-citationLi, J., Baud, O., Vartanian, T. K., Volpe, J. J., & Rosenberg, P. A. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0502552102 · Cited by 370 · see citing works
NADPH Oxidases of the Brain: Distribution, Regulation, and Function
Infanger, D. W., Sharma, R. V., & Davisson, R. L. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.1583 · Cited by 362 · 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
A local mechanism mediates NAD-dependent protection of axon degeneration
Wang, J., Zhai, Q., Chen, Y., Lin, E., Gu, W., McBurney, M. W., & He, Z. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200504028 · Cited by 352 · see citing works
Ischemic stroke injury is reduced in mice lacking a functional NADPH oxidase
Walder, C. E., Green, S. P., Darbonne, W. C., Mathias, J., Rae, J., Dinauer, M. C., Curnutte, J. T., & Thomas, G. R. (1997) · Stroke · doi:10.1161/01.str.28.11.2252 · Cited by 349 · see citing works
Tryptophan metabolism and brain function: focus on kynurenine and other indole metabolites
Moroni, F. (1999) · European Journal of Pharmacology · doi:10.1016/s0014-2999(99)00196-x · Cited by 347 · see citing works
Cellular thiols and redox-regulated signal transduction
Sen, C. K. (2001) · Current topics in cellular regulation · doi:10.1016/s0070-2137(01)80001-7 · Cited by 345 · see citing works
NADPH oxidase-dependent redox signalling in cardiac hypertrophy, remodelling and failure
Murdoch, C. E., Zhang, M., Cave, A. C., & Shah, A. M. (2006) · Cardiovascular Research · doi:10.1016/j.cardiores.2006.03.016 · Cited by 343 · see citing works
NAD(P)H, a directly operating antioxidant?
Kirsch, M., & de GROOT, H. (2001) · The FASEB Journal · doi:10.1096/fj.00-0823hyp · Cited by 331 · see citing works
SIRT1 Regulates HIV Transcription via Tat Deacetylation
Pagans, S., Pedal, A., North, B. J., Kaehlcke, K., Marshall, B. L., Dorr, A., Hetzer‐Egger, C., Henklein, P., Frye, R. A., McBurney, M. W., et al. (2005) · PLoS Biology · doi:10.1371/journal.pbio.0030041 · Cited by 330 · see citing works
Cohen-Armon, M., Visochek, L., Rozensal, D., Kalal, A., Geistrikh, I., Klein, R., Bendetz-Nezer, S., Yao, Z., & Seger, R. (2007) · Molecular Cell · doi:10.1016/j.molcel.2006.12.012 · Cited by 329 · see citing works
McKenna, M. C., Waagepetersen, H. S., Schousboe, A., & Sonnewald, U. (2006) · Biochemical Pharmacology · doi:10.1016/j.bcp.2005.10.011 · Cited by 328 · see citing works
Importance of Poly(ADP-Ribose) Glycohydrolase in the Control of Poly(ADP-Ribose) Metabolism
Davidovic, L., Vodenicharov, M. D., Affar, E. B., & Poirier, G. G. (2001) · Experimental Cell Research · doi:10.1006/excr.2001.5263 · Cited by 326 · see citing works
Extension of Human Cell Lifespan by Nicotinamide Phosphoribosyltransferase
van der Veer, E., Ho, C. S. W., O’Neil, C. H., Barbosa, N., Scott, R., Cregan, S. P., & Pickering, J. G. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.c700018200 · Cited by 325 · see citing works
Apoptosis-inducing factor: vital and lethal
Modjtahedi, N., Giordanetto, F., Madeo, F., & Kroemer, G. (2006) · Trends in Cell Biology · doi:10.1016/j.tcb.2006.03.008 · Cited by 323 · see citing works
Sawa, A., Khan, A. A., Hester, L. D., & Snyder, S. H. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.21.11669 · Cited by 316 · see citing works
The regulation of nicotinamide adenine dinucleotide biosynthesis by Nampt/PBEF/visfatin in mammals
Revollo, J. R., Grimm, A. A., & Imai, S. (2007) · Current Opinion in Gastroenterology · doi:10.1097/mog.0b013e32801b3c8f · Cited by 311 · see citing works
Du, L., Zhang, X., Han, Y. Y., Burke, N. A., Kochanek, P. M., Watkins, S. C., Graham, S. H., Carcillo, J. A., Szabó, C., & Clark, R. S. B. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301295200 · Cited by 310 · see citing works
Grube, K., & Bürkle, A. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.24.11759 · Cited by 301 · see citing works
GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE, APOPTOSIS, AND NEURODEGENERATIVE DISEASES
Chuang, D., Hough, C. J., & Senatorov, V. V. (2004) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.45.120403.095902 · Cited by 301 · see citing works
Poly(ADP-ribose) polymerase-deficient mice are protected from streptozotocin-induced diabetes
Pieper, A. A., Brat, D. J., Krug, D. K., Watkins, C. C., Gupta, A., Blackshaw, S., Verma, A. M., Wang, Z., & Snyder, S. H. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.6.3059 · Cited by 298 · see citing works
The Enzymatic and DNA Binding Activity of PARP-1 Are Not Required for NF-κB Coactivator Function
Hassa, P. O., Covic, M., Hasan, S., Imhof, R., & Hottiger, M. O. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106528200 · Cited by 296 · see citing works
Cancer-Specific Functions of SIRT1 Enable Human Epithelial Cancer Cell Growth and Survival
Ford, J. R., Jiang, M., & Milner, J. (2005) · Cancer Research · doi:10.1158/0008-5472.can-05-1923 · Cited by 295 · see citing works
Bürkle, A. (2005) · FEBS Journal · doi:10.1111/j.1742-4658.2005.04864.x · Cited by 294 · see citing works
Functional aspects of protein mono‐ADP‐ribosylation
Corda, D., & Girolamo, M. D. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg209 · Cited by 294 · see citing works
Activation of NADPH Oxidase in Alzheimer’s Disease Brains
Shimohama, S., Tanino, H., Kawakami, N., Okamura, N., Kodama, H., Yamaguchi, T., Hayakawa, T., Nunomura, A., Chiba, S., Perry, G., et al. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.2897 · Cited by 292 · see citing works
New functions of a long‐known molecule
Ziegler, M. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01187.x · Cited by 289 · see citing works
Enzymology of NAD+ homeostasis in man
Magni, G., Amici, A., Emanuelli, M., Orsomando, G., Raffaelli, N., & Ruggieri, S. (2004) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-003-3161-1 · Cited by 289 · see citing works
Fonfría, E., Marshall, I. C. B., Benham, C. D., Boyfield, I., Brown, J. D., Hill, K., Hughes, J. P., Skaper, S. D., & McNulty, S. (2004) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0705914 · Cited by 283 · see citing works
Chi, N., & Lodish, H. F. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m007635200 · Cited by 277 · see citing works
Beal, M. F. (2004) · Journal of Bioenergetics and Biomembranes · doi:10.1023/b:jobb.0000041772.74810.92 · Cited by 276 · see citing works
The superoxide‐producing NAD(P)H oxidase Nox4 in the nucleus of human vascular endothelial cells
Kuroda, J., Nakagawa, K., Yamasaki, T., Nakamura, K., Takeya, R., Kuribayashi, F., Imajoh‐Ohmi, S., Igarashi, K., Shibata, Y., Sueishi, K., et al. (2005) · Genes to Cells · doi:10.1111/j.1365-2443.2005.00907.x · Cited by 275 · see citing works
NAD + as a metabolic link between DNA damage and cell death
Ying, W., Alano, C. C., Garnier, P. E., & Swanson, R. A. (2004) · Journal of Neuroscience Research · doi:10.1002/jnr.20289 · Cited by 269 · see citing works
Self-citationNitric Oxide Modulates Superoxide Release and Peroxynitrite Formation in Human Blood Vessels
Guzik, T. J., West, N. E. J., Pillai, R. G., Taggart, D. P., & Channon, K. M. (2002) · Hypertension · doi:10.1161/01.hyp.0000018041.48432.b5 · Cited by 264 · see citing works
Mitochondrial NADPH, transhydrogenase and disease
Rydström, J. (2006) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2006.03.010 · Cited by 256 · see citing works
Ha, H. C., Hester, L. D., & Snyder, S. H. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.052712399 · Cited by 255 · see citing works
Role of Nox Family NADPH Oxidases in Host Defense
Leto, T. L., & Geiszt, M. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.1549 · Cited by 254 · see citing works
The parkinsonian toxin MPTP: action and mechanism
Przedborski, S., Jackson-Lewis, V. R., Djaldetti, R., Liberatore, G. T., Vila, M., Vukosavić, S., & Almer, G. (2000) · Restorative Neurology and Neuroscience · doi:10.3233/rnn-2000-00132 · Cited by 253 · see citing works
Cytosolic NADP+-dependent Isocitrate Dehydrogenase Plays a Key Role in Lipid Metabolism
Koh, H., Lee, S., Son, B.-G., Lee, S.-H., Ryoo, Z. Y., Chang, K., Park, J., Park, D., Song, B. J., Veech, R. L., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402260200 · Cited by 253 · see citing works
NAD+ and NADH in cellular functions and cell death
Ying, W. (2006) · Frontiers in bioscience · doi:10.2741/2038 · Cited by 250 · see citing works
Self-citationCalcium as sculptor and destroyer of neural circuitry
Mattson, M. P. (1992) · Experimental Gerontology · doi:10.1016/0531-5565(92)90027-w · Cited by 250 · see citing works
Neuroprotection by pharmacologic blockade of the GAPDH death cascade
Hara, M. R., Thomas, B., Cascio, M. B., Bae, B.-I., Hester, L. D., Dawson, V. L., Dawson, T. M., Sawa, A., & Snyder, S. H. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0511321103 · Cited by 238 · see citing works
Magni, G., Amici, A., Emanuelli, M., Raffaelli, N., & Ruggieri, S. (1999) · Advances in enzymology and related areas of molecular biology/Advances in enzymology and related subjects · doi:10.1002/9780470123195.ch5 · Cited by 235 · see citing works
Xu, Y., Huang, S., Liu, Z. G., & Han, J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m508135200 · Cited by 235 · see citing works
Wang, Q., Tompkins, K. D., Simonyi, Á., Korthuis, R. J., Sun, A. Y., & Sun, G. Y. (2006) · Brain Research · doi:10.1016/j.brainres.2006.03.060 · Cited by 235 · see citing works
Ronnebaum, S. M., Ilkayeva, O., Burgess, S. C., Joseph, J. W., Lu, D., Stevens, R. D., Becker, T. C., Sherry, A. D., Newgard, C. B., & Jensen, M. V. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m511908200 · Cited by 230 · see citing works
Identification of the Mitochondrial NAD+ Transporter in Saccharomyces cerevisiae
Todisco, S., Agrimi, G., Castegna, A., & Palmieri, F. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m510425200 · Cited by 223 · see citing works
The mitochondrial permeability transition pore
Crompton, M., Virji, S., Doyle, V., Johnson, N., & Ward, J. M. (1999) · Biochemical Society Symposia · doi:10.1042/bss0660167 · Cited by 222 · see citing works
Slekar, K. H., Kosman, D. J., & Culotta, V. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.46.28831 · Cited by 216 · see citing works
Keller, J. N., Guo, Q., Holtsberg, F. W., Bruce‐Keller, A. J., & Mattson, M. P. (1998) · Journal of Neuroscience · doi:10.1523/jneurosci.18-12-04439.1998 · Cited by 214 · see citing works
Suh, S. W., Aoyama, K., Chen, Y., Garnier, P. E., Matsumori, Y., Gum, E. T., Liu, J., & Swanson, R. A. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-33-10681.2003 · Cited by 210 · see citing works
Early Steps in the Biosynthesis of NAD in Arabidopsis Start with Aspartate and Occur in the Plastid
Katoh, A., Uenohara, K., Akita, M., & Hashimoto, T. (2006) · PLANT PHYSIOLOGY · doi:10.1104/pp.106.081091 · Cited by 210 · see citing works
Kauppinen, T. M., Chan, W., Suh, S. W., Wiggins, A. K., Huang, E. J., & Swanson, R. A. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0508606103 · Cited by 208 · see citing works
Sazanov, L. A., & Jackson, J. B. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00370-x · Cited by 205 · see citing works
Kolthur‐Seetharam, U., Dantzer, F., McBurney, M. W., de MURCIA, G., & Sassone‐Corsi, P. (2006) · Cell Cycle · doi:10.4161/cc.5.8.2690 · Cited by 203 · see citing works
Fonfría, E., Marshall, I. C. B., Boyfield, I., Skaper, S. D., Hughes, J. P., OWEN, D. E., Zhang, W., Miller, B. A., Benham, C. D., & McNulty, S. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03396.x · Cited by 202 · see citing works
Ying, W., Garnier, P. E., & Swanson, R. A. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)01483-9 · Cited by 202 · see citing works
Self-citationAcetylation of TAFI68, a subunit of TIF‐IB/SL1, activates RNA polymerase I transcription
Muth, V., Nadaud, S., Grummt, I., & Voit, R. (2001) · The EMBO Journal · doi:10.1093/emboj/20.6.1353 · Cited by 201 · see citing works
Poly(ADP-ribose) glycohydrolase mediates oxidative and excitotoxic neuronal death
Ying, W., Sevigny, M. B., Chen, Y., & Swanson, R. A. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.211202598 · Cited by 199 · see citing works
Self-citationAnderson, J. M., Charbonneau, H., Jones, H. P., et al. (1980) · Biochemistry · doi:10.1021/bi00554a043 · Cited by 192 · see citing works
A novel NADH kinase is the mitochondrial source of NADPH in Saccharomyces cerevisiae
Outten, C. E., & Culotta, V. C. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg211 · Cited by 189 · see citing works
Wolin, M. S., Ahmad, M., & Gupte, S. A. (2005) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00060.2005 · Cited by 188 · see citing works
Nicotinamide: necessary nutrient emerges as a novel cytoprotectant for the brain
Maiese, K., & Chong, Z. Z. (2003) · Trends in Pharmacological Sciences · doi:10.1016/s0165-6147(03)00078-6 · Cited by 187 · see citing works
van der Veer, E., Nong, Z., O’Neil, C. H., Urquhart, B. L., Freeman, D. J., & Pickering, J. G. (2005) · Circulation Research · doi:10.1161/01.res.0000173298.38808.27 · Cited by 187 · see citing works
Aswad, F., Kawamura, H., & Dennert, G. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.175.5.3075 · Cited by 183 · see citing works
Dueling Activities of AIF in Cell Death versus Survival
Lipton, S. A., & Bossy‐Wetzel, E. (2002) · Cell · doi:10.1016/s0092-8674(02)01046-2 · Cited by 180 · see citing works
Beck, A., Kolísek, M., Bagley, L. A., Fleig, A., & Penner, R. (2006) · The FASEB Journal · doi:10.1096/fj.05-5538fje · Cited by 175 · see citing works
Structural and Functional Characterization of Human NAD Kinase
Lerner, F., Niere, M., Ludwig, A., & Ziegler, M. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.5735 · Cited by 172 · see citing works
Tankyrase 1 as a target for telomere-directed molecular cancer therapeutics
Seimiya, H., Muramatsu, Y., Ohishi, T., & Tsuruo, T. (2005) · Cancer Cell · doi:10.1016/j.ccr.2004.11.021 · Cited by 166 · see citing works
Drosophila NMNAT Maintains Neural Integrity Independent of Its NAD Synthesis Activity
Zhai, R. G., Cao, Y., Hiesinger, P. R., Zhou, Y., Mehta, S. Q., Schulze, K. L., Verstreken, P., & Bellen, H. J. (2006) · PLoS Biology · doi:10.1371/journal.pbio.0040416 · Cited by 166 · see citing works
Identification of a Plasmid-Encoded Gene from Haemophilus ducreyi Which Confers NAD Independence
Martin, P. R., Shea, R. J., & Mulks, M. H. (2001) · Journal of Bacteriology · doi:10.1128/jb.183.4.1168-1174.2001 · Cited by 165 · see citing works
Zhang, D., & Armstrong, J. S. (2006) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402072 · Cited by 165 · see citing works
Kim, Y.-H., & Koh, J.-Y. (2002) · Experimental Neurology · doi:10.1006/exnr.2002.7990 · Cited by 163 · see citing works
Hypoxic pulmonary vasoconstriction: redox events in oxygen sensing
Waypa, G. B., & Schumacker, P. T. (2004) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00722.2004 · Cited by 162 · see citing works
Pathophysiological relevance of mitochondria in NAD+ metabolism
Lisa, F. D., & Ziegler, M. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02198-6 · Cited by 161 · see citing works
Kaneko, S., Wang, J., Kaneko, M., Yiu, G. C., Hurrell, J., Chitnis, T., Khoury, S. J., & He, Z. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.2116-06.2006 · Cited by 159 · see citing works
Cecchi, C., Fiorillo, C., Sorbi, S., Latorraca, S., Nacmias, B., Bagnoli, S., Nassi, P., & Liguri, G. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01049-3 · Cited by 159 · see citing works
The role of an astrocytic NADPH oxidase in the neurotoxicity of amyloid beta peptides
Abramov, A. Y., & Duchen, M. R. (2005) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2005.1766 · Cited by 158 · see citing works
Poly(ADP-ribose) polymerase enhances activator-dependent transcription in vitro
Meisterernst, M., Stelzer, G., & Roeder, R. G. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.6.2261 · Cited by 155 · see citing works
Metabolite of SIR2 Reaction Modulates TRPM2 Ion Channel
Grubisha, O., Rafty, L. A., Takanishi, C. L., Xu, X., Tong, L., Perraud, A., Scharenberg, A. M., & Denu, J. M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m513741200 · Cited by 154 · see citing works
Modulation of DNMT1 activity by ADP-ribose polymers
Reale, A., MATTEIS, G. D., Galleazzi, G., et al. (2005) · Oncogene · doi:10.1038/sj.onc.1208005 · Cited by 150 · see citing works
Control of the redox state of the nicotinamide–adenine dinucleotide couple in rat liver cytoplasm
Stubbs, M., Veech, R. L., & Krebs, H. A. (1972) · Biochemical Journal · doi:10.1042/bj1260059 · Cited by 149 · see citing works
Kühn, F. J. P., Heiner, I., & Lückhoff, A. (2005) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-005-1446-y · Cited by 148 · see citing works
Mhatre, M., Floyd, R. A., & Hensley, K. (2004) · Journal of Alzheimer s Disease · doi:10.3233/jad-2004-6206 · Cited by 147 · see citing works
SIRT1 interacts with p73 and suppresses p73‐dependent transcriptional activity
Dai, J. M., Wang, Z. Y., Sun, D. C., Lin, R. X., & Wang, S. Q. (2006) · Journal of Cellular Physiology · doi:10.1002/jcp.20831 · Cited by 147 · see citing works
Scott, M., Zuo, L., Lubin, B. H., & Chiu, D. (1991) · Blood · doi:10.1182/blood.v77.9.2059.2059 · Cited by 142 · see citing works
Role of Telomeres and Telomerase in the Pathogenesis of Human Cancer
Hahn, W. C. (2003) · Journal of Clinical Oncology · doi:10.1200/jco.2003.06.018 · Cited by 141 · see citing works
Chong, Z. Z., Lin, S., & Maiese, K. (2004) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1097/01.wcb.0000122746.72175.0e · Cited by 140 · see citing works
von Kobbe, C., Harrigan, J. A., May, A., Opresko, P. L., Dawut, L., Cheng, W., & Bohr, V. A. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.23.8601-8613.2003 · Cited by 140 · see citing works
Guse, A. H. (2005) · The FEBS Journal · doi:10.1111/j.1742-4658.2005.04863.x · Cited by 139 · see citing works
Martín‐Oliva, D., Aguilar‐Quesada, R., O’Valle, F., Muñoz‐Gámez, J. A., Martínez‐Romero, R., del Moral, R. G., de Almodóvar, J. M. R., Villuendas, R., Piris, M. A., & Oliver, F. J. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-3050 · Cited by 138 · see citing works
Dehydroepiandrosterone, glucose-6-phosphate dehydrogenase, and longevity
Schwartz, A. (2004) · Ageing Research Reviews · doi:10.1016/j.arr.2003.05.001 · Cited by 136 · see citing works
Conforti, L., Fang, G., Beirowski, B., Wang, M. S., Sorci, L., Asress, S., Adalbert, R., Silva, A., Bridge, K., Huang, X. P., et al. (2006) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401944 · Cited by 136 · see citing works
Grabowska, D., & Chełstowska, A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210076200 · Cited by 136 · see citing works
Pyruvate Administered After Severe Hypoglycemia Reduces Neuronal Death and Cognitive Impairment
Suh, S. W., Aoyama, K., Matsumori, Y., Liu, J., & Swanson, R. A. (2005) · Diabetes · doi:10.2337/diabetes.54.5.1452 · Cited by 135 · see citing works
Chang, W.-J., & Álvarez-González, R. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104666200 · Cited by 134 · see citing works
Nakae, J. (2006) · Journal of Clinical Investigation · doi:10.1172/jci25518 · Cited by 132 · see citing works
Mokudai, T., Ayoub, I. A., Sakakibara, Y., Lee, E.-J., Ogilvy, C. S., & Maynard, K. I. (2000) · Stroke · doi:10.1161/01.str.31.7.1679 · Cited by 131 · see citing works
Yakovlev, A. G., Wang, G., Stoica, B. A., Boulares, H. A., Spoonde, A. Y., Yoshihara, K., & Smulson, M. E. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001087200 · Cited by 131 · see citing works
Tricarboxylic Acid Cycle Substrates Prevent PARP-Mediated Death of Neurons and Astrocytes
Ying, W., Chen, Y., Alano, C. C., & Swanson, R. A. (2002) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1097/00004647-200207000-00002 · Cited by 130 · see citing works
Self-citationOxidative Stress: The Old Enemy in Alzheimers Disease Pathophysiology
Moreira, P. I., Honda, K., Liu, Q., Santos, M. S., Oliveira, C. R., Aliev, G., Nunomura, A., Zhu, X., Smith, M. A., & Perry, G. L. (2005) · Current Alzheimer Research · doi:10.2174/156720505774330537 · Cited by 129 · see citing works
Verderio, C., Bruzzone, S., Zocchi, E., Fedele, E., Schenk, U., FLORA, A. D., & Matteoli, M. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00455.x · Cited by 128 · see citing works
LaPlaca, M. C., Zhang, J., Raghupathi, R., Li, J., Smith, F. M., Bareyre, F. M., Snyder, S. H., Graham, D. I., & McIntosh, T. K. (2001) · Journal of Neurotrauma · doi:10.1089/089771501750170912 · Cited by 127 · see citing works
Identification of a novel human nicotinamide mononucleotide adenylyltransferase
Raffaelli, N., Sorci, L., Amici, A., Emanuelli, M., Mazzola, F., & Magni, G. (2002) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)02285-4 · Cited by 127 · see citing works
Role of AT1 receptors and NAD(P)H oxidase in diabetes-aggravated ischemic brain injury
Kusaka, I., Kusaka, G., Zhou, C., Ishikawa, M., Nanda, A., Granger, D. N., Zhang, J. H., & Tang, J. (2004) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.01169.2003 · Cited by 127 · see citing works
Sapko, M. T., Guidetti, P., Yu, P., Tagle, D., Pellicciari, R., & Schwarcz, R. (2006) · Experimental Neurology · doi:10.1016/j.expneurol.2005.07.004 · Cited by 127 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Hayes, J. D., Dinkova-Kostova, A. T., & Tew, K. D. (2020) · Cancer Cell · doi:10.1016/j.ccell.2020.06.001 · Cited by 2,654 · see citing works
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+ in Brain Aging and Neurodegenerative Disorders
Lautrup, S., Sinclair, D. A., Mattson, M. P., & Fang, E. F. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2019.09.001 · Cited by 790 · see citing works
PARPs and ADP-ribosylation: recent advances linking molecular functions to biological outcomes
Gupte, R., Liu, Z., & Kraus, W. L. (2017) · Genes & Development · doi:10.1101/gad.291518.116 · Cited by 681 · 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
Redox regulation of mitochondrial function
Handy, D. E., & Loscalzo, J. (2012) · Antioxidants & Redox Signaling · doi:10.1089/ars.2011.4123 · Cited by 588 · see citing works
Increased demand for NAD(+) relative to ATP drives aerobic glycolysis
Luengo, A., Li, Z., Gui, D. Y., Sullivan, L. B., Zagorulya, M., Do, B. T., Ferreira, R., Naamati, A., Ali, A., Lewis, C. A., et al. (2021) · Molecular Cell · doi:10.1016/j.molcel.2020.12.012 · Cited by 547 · see citing works
Mammalian Mitochondrial Complex I: Biogenesis, Regulation, and Reactive Oxygen Species Generation
Koopman, W. J. H., Nijtmans, L. G. J., Dieteren, C. E. J., Roestenberg, P., Valsecchi, F., Smeitink, J. A. M., & Willems, P. H. G. M. (2010) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2743 · Cited by 411 · see citing works
Münzel, T., Gori, T., Keaney, J. F., Maack, C., & Daiber, A. (2015) · European Heart Journal · doi:10.1093/eurheartj/ehv305 · Cited by 394 · see citing works
Sasaki, M., Knobbe, C. B., Itsumi, M., Elia, A. J., Harris, I. S., Chio, I. I. C., Cairns, R. A., McCracken, S., Wakeham, A., Haight, J., et al. (2012) · Genes & Development · doi:10.1101/gad.198200.112 · Cited by 296 · see citing works
Exercise alters SIRT1, SIRT6, NAD and NAMPT levels in skeletal muscle of aged rats
Koltai, E., Szabo, Z., Atalay, M., Boldogh, I., Naito, H., Goto, S., Nyakas, C., & Radak, Z. (2010) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2009.11.002 · Cited by 283 · see citing works
Inhibition of nicotinamide phosphoribosyltransferase (NAMPT) as a therapeutic strategy in cancer
Sampath, D., Zabka, T. S., Misner, D. L., O’Brien, T., & Dragovich, P. S. (2015) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2015.02.004 · Cited by 258 · see citing works
Engin, A. B. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-48382-5_8 · Cited by 260 · see citing works
Nielsen, J. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-044757 · Cited by 252 · see citing works
Wang, X., Hu, X., Yang, Y., Takata, T., & Sakurai, T. (2016) · Brain Research · doi:10.1016/j.brainres.2016.04.060 · Cited by 217 · see citing works
Dröse, S. (2013) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2013.01.004 · Cited by 201 · see citing works
Sources and implications of NADH/NAD+ redox imbalance in diabetes and its complications
Yan, L.-J., Wu, J., Jin, Z., & Zheng, H. (2016) · Diabetes, Metabolic Syndrome and Obesity: Targets and Therapy · doi:10.2147/dmso.s106087 · Cited by 198 · see citing works
Skeletal muscle stem cells adopt a dormant cell state post mortem and retain regenerative capacity
Latil, M., Rocheteau, P., Châtre, L., Sanulli, S., Mémet, S., Ricchetti, M., Tajbakhsh, S., & Chrétien, F. (2012) · Nature Communications · doi:10.1038/ncomms1890 · Cited by 165 · see citing works
Thioredoxin and Thioredoxin Reductase in Relation to Reversible <i>S</i> -Nitrosylation
Sengupta, R., & Holmgren, A. (2013) · Antioxidants & Redox Signaling · doi:10.1089/ars.2012.4716 · Cited by 156 · 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
Interactions between epigenetics and metabolism in cancers
Yun, J., Johnson, J. L., Hanigan, C. L., & Locasale, J. W. (2012) · Frontiers in Oncology · doi:10.3389/fonc.2012.00163 · Cited by 82 · see citing works
Haddad, M., Hervé, V., Ben Khedher, M. R., Rabanel, J.-M., & Ramassamy, C. (2021) · Antioxidants & Redox Signaling · doi:10.1089/ars.2020.8129 · Cited by 68 · see citing works
Marcu, R., Wiczer, B. M., Neeley, C. K., & Hawkins, B. J. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.00068-14 · Cited by 62 · see citing works
Skin Redox Balance Maintenance: The Need for an Nrf2-Activator Delivery System
Ben-Yehuda Greenwald, M., Ben-Sasson, S., Bianco-Peled, H., & Kohen, R. (2016) · Cosmetics · doi:10.3390/cosmetics3010001 · Cited by 49 · see citing works
Ren, Z., Xu, Y., Li, T., Sun, W., Tang, Z., Wang, Y., Zhou, K., Li, J., Ding, Q., Liang, K., et al. (2022) · Animal Nutrition · doi:10.1016/j.aninu.2022.06.009 · Cited by 44 · see citing works
Kim, N., Jung, Y., Nam, M., Sun Kang, M., Lee, M. K., Cho, Y., Choi, E.-K., Hwang, G.-S., & Soo Kim, H. (2017) · Scientific Reports · doi:10.1038/s41598-017-09675-3 · Cited by 39 · see citing works
Inhibition of NAMPT decreases cell growth and enhances susceptibility to oxidative stress
Xu, R., Yuan, Z., Yang, L., Li, L., Li, D., & Lv, C. (2017) · Oncology Reports · doi:10.3892/or.2017.5793 · Cited by 36 · see citing works
Zou, Y., Wang, R., Guo, H., & Dong, M. (2015) · Toxicological Sciences · doi:10.1093/toxsci/kfv111 · Cited by 36 · see citing works
Conley, K. E., Ali, A. S., Flores, B., Jubrias, S. A., & Shankland, E. G. (2016) · Frontiers in Physiology · doi:10.3389/fphys.2016.00045 · Cited by 22 · see citing works
- Authors
- Ying, W.
- Affiliations
- San Francisco VA Medical Center (US)
- Corresponding author
- Ying, Weihai
- ORCID
- Ying, Weihai
- Venue
- Antioxidants & Redox Signaling
- Publisher
- SAGE Publications
- Published
- 2008-02
- Volume
- 10
- Issue
- 2
- Pages
- 179-206
- ISSN
- 1523-0864 (ISSN-L)
- 1557-7716
- OpenAlex
- W1970554352
- Cited by
- 1,494
- References
- 339
- Citations by year
- 2026: 80 · 2025: 106 · 2024: 94 · 2023: 103 · 2022: 120 · 2021: 138 · 2020: 103 · 2019: 89 · 2018: 76 · 2017: 91 · 2016: 101 · 2015: 82 · 2014: 65 · 2013: 59 · 2012: 56
- FWCI
- 13.05
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Antioxidants and Redox Signaling (publishedVersion)
- PubMed (publishedVersion)
- 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+, NADH, NADPH, cell death, energy metabolism, mitochondrial function, calcium homeostasis, reactive oxygen species, oxidative stress, anti-oxidation, cyclic ADP-ribose, mitochondrial permeability transition, PARP1, apoptosis-inducing factor, aging, sirtuins
- MeSH terms
- Animals, Cell Physiological Phenomena, Energy Metabolism, Homeostasis, Humans, Mitochondria, NAD, NADP, Oxidation-Reduction, Cell Death
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