Crosstalk between poly(ADP-ribose) polymerase and sirtuin enzymes
Open accessAbstract
Poly(ADP-ribose) polymerases (PARPs) are NAD(+) dependent enzymes that were identified as DNA repair proteins, however, today it seems clear that PARPs are responsible for a plethora of biological functions. Sirtuins (SIRTs) are NAD(+)-dependent deacetylase enzymes involved in the same biological processes as PARPs raising the question whether PARP and SIRT enzymes may interact with each other in physiological and pathophysiological conditions. Hereby we review the current understanding of the SIRT-PARP interplay in regard to the biochemical nature of the interaction (competition for the common NAD(+) substrate, mutual posttranslational modifications and direct transcriptional effects) and the physiological or pathophysiological consequences of the interactions (metabolic events, oxidative stress response, genomic stability and aging). Finally, we give an overview of the possibilities of pharmacological intervention to modulate PARP and SIRT enzymes either directly, or through modulating NAD(+) homeostasis.
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Poly-ADP-ribose chains act as a scaffold for repair proteins, ensuring effective recruitment of SSBR and DSBR machinery.
“Poly-ADP-ribose chains act as a scaffold for repair proteins, ensuring effective recruitment of single-strand break repair (SSBR) and double-strand break repair (DSBR) machinery.”
From Focus on UV-Induced DNA Damage and Repair—Disease Relevance and Protective Strategies (2020) · cites this paper as [66]
PARPs catalyze a conserved posttranslational modification transferring ADP-ribose residues from NAD+ onto amino acid moieties of various proteins, including histones and PARP itself, forming poly-ADP-ribose chains.
“PARPs catalyze an evolutionary conserved posttranslational modification in which ADP-ribose residues from nicotinamide adenine dinucleotide (NAD+) molecules are transferred onto amino acid moieties of various proteins, including histone proteins and PARP itself, leading to polymeric ADP-ribose chains formation.”
From Focus on UV-Induced DNA Damage and Repair—Disease Relevance and Protective Strategies (2020) · cites this paper as [66]
PARPs work as signaling molecules in single-strand break repair.
“In contrast, poly [ADP-ribose] polymerases (PARPs) work as signaling molecules in single-strand break repair.”
From Focus on UV-Induced DNA Damage and Repair—Disease Relevance and Protective Strategies (2020) · cites this paper as [66]
PARP1 and PARP2 are the main enzymes with a function in damage signaling.
“PARP1 and PARP2 are the main enzymes with a function in damage signaling.”
From Focus on UV-Induced DNA Damage and Repair—Disease Relevance and Protective Strategies (2020) · cites this paper as [66]
PAR chains are rapidly disassembled by PARG, allowing the whole event to repeat.
“Poly-ADP-ribose (PAR) chains are rapidly disassembled by poly (ADP-ribose) glycohydrolase (PARG), allowing the whole event to repeat [55,66].”
From Focus on UV-Induced DNA Damage and Repair—Disease Relevance and Protective Strategies (2020) · cites this paper as [66]
PARP binding is only temporary due to emerging electrostatic interactions.
“PARP binding is only temporary due to emerging electrostatic interactions.”
From Focus on UV-Induced DNA Damage and Repair—Disease Relevance and Protective Strategies (2020) · cites this paper as [66]
PARP1 is responsible for the majority of ADP-ribosylation events in the cell.
“In fact, PARP1 is responsible for the majority of ADP-ribosylation events in cell.”
From Focus on UV-Induced DNA Damage and Repair—Disease Relevance and Protective Strategies (2020) · cites this paper as [66]
PARP1 likely outcompetes SIRT1 for NAD+ because PARP1 has lower Km and higher Vmax for NAD+ than SIRT1, and they are localized to the same cellular compartment.
“However, since PARP1 has lower Km and higher Vmax with regard to NAD+ than SIRT1, PARP1 likely outcompetes SIRT1 for NAD+ as a result of its greater binding affinity and faster kinetics34.”
From NAD+ metabolism and its roles in cellular processes during ageing (2021) · cites this paper as [34]
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2 retracted
Age related changes in NAD+ metabolism oxidative stress and Sirt1 activity in wistar rats
Braidy, N., Guillemin, G. J., Mansour, H., Chan-Ling, T., Poljak, A., & Grant, R. (2011) · PLoS ONE · doi:10.1371/journal.pone.0019194 · Cited by 594 · see citing works
RetractedRETRACTED: Metabolic regulation of SIRT1 transcription via a HIC1:CtBP corepressor complex
Zhang, Q., Wang, S.-Y., Fleuriel, C., Leprince, D., Rocheleau, J. V., Piston, D. W., & Goodman, R. H. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0610590104 · Cited by 171 · see citing works
RetractedNitric Oxide and Peroxynitrite in Health and Disease
Pacher, P., Beckman, J. S., & Liaudet, L. (2007) · Physiological Reviews · doi:10.1152/physrev.00029.2006 · Cited by 6,390 · see citing works
Trumbo (2001) · doi:10.1016/s0002-8223(01)00078-5 · Cited by 4,852 · see citing works
Nitric oxide synthases: regulation and function
Forstermann, U., & Sessa, W. C. (2012) · European Heart Journal · doi:10.1093/eurheartj/ehr304 · Cited by 4,409 · see citing works
Reactive oxygen species (ROS) homeostasis and redox regulation in cellular signaling
Ray, P. D., Huang, B.-W., & Tsuji, Y. (2012) · Cellular Signalling · doi:10.1016/j.cellsig.2012.01.008 · Cited by 4,373 · see citing works
Nitric oxide as a secretory product of mammalian cells
Nathan, C. (1992) · The FASEB Journal · doi:10.1096/fasebj.6.12.1381691 · Cited by 4,350 · see citing works
Resveratrol improves health and survival of mice on a high-calorie diet
Baur, J. A., Pearson, K. J., Price, N. L., Jamieson, H. A., Lerin, C., Kalra, A., Prabhu, V. V., Allard, J. S., Lopez-Lluch, G., Lewis, K., et al. (2006) · Nature · doi:10.1038/nature05354 · Cited by 4,290 · see citing works
Lagouge, M., Argmann, C., Gerhart-Hines, Z., Meziane, H., Lerin, C., Daussin, F., Messadeq, N., Milne, J., Lambert, P., Elliott, P., et al. (2006) · Cell · doi:10.1016/j.cell.2006.11.013 · Cited by 4,057 · see citing works
Small molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan
Howitz, K. T., Bitterman, K. J., Cohen, H. Y., Lamming, D. W., Lavu, S., Wood, J. G., Zipkin, R. E., Chung, P., Kisielewski, A., Zhang, L.-L., et al. (2003) · Nature · doi:10.1038/nature01960 · Cited by 3,796 · see citing works
Inhibition of Poly(ADP-Ribose) Polymerase in Tumors from <i>BRCA</i> Mutation Carriers
Fong, P. C., Boss, D. S., Yap, T. A., Tutt, A., Wu, P., Mergui-Roelvink, M., Mortimer, P., Swaisland, H., Lau, A., O'Connor, M. J., et al. (2009) · New England Journal of Medicine · doi:10.1056/nejmoa0900212 · Cited by 3,634 · see citing works
Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
Imai, S.-I., Armstrong, C. M., Kaeberlein, M., & Guarente, L. (2000) · Nature · doi:10.1038/35001622 · Cited by 3,510 · see citing works
AMPK regulates energy expenditure by modulating NAD+ metabolism and SIRT1 activity
Cantó, C., Gerhart-Hines, Z., Feige, J. N., Lagouge, M., Noriega, L., Milne, J. C., Elliott, P. J., Puigserver, P., & Auwerx, J. (2009) · Nature · doi:10.1038/nature07813 · Cited by 3,300 · see citing works
Self-citationStress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase
Brunet, A., Sweeney, L. B., Sturgill, J. F., Chua, K. F., Greer, P. L., Lin, Y., Tran, H., Ross, S. E., Mostoslavsky, R., Cohen, H. Y., et al. (2004) · Science · doi:10.1126/science.1094637 · Cited by 3,239 · 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
hSIR2SIRT1 Functions as an NAD-Dependent p53 Deacetylase
Vaziri, H., Dessain, S. K., Eaton, E. N., Imai, S., Frye, R. A., Pandita, T. K., Guarente, L., & Weinberg, R. A. (2001) · Cell · doi:10.1016/s0092-8674(01)00527-x · Cited by 2,653 · see citing works
Transcriptional co-activator PGC-1α drives the formation of slow-twitch muscle fibres
Lin, J., Wu, H., Tarr, P. T., Zhang, C.-Y., Wu, Z., Boss, O., Michael, L. F., Puigserver, P., Isotani, E., Olson, E. N., et al. (2002) · Nature · doi:10.1038/nature00904 · Cited by 2,546 · see citing works
Tewari, M., Quan, L. T., O’Rourke, K. M., Desnoyers, S., Zeng, Z., Beidler, D. R., Poirier, G. G., Salvesen, G. S., & Dixit, V. M. (1995) · Cell · doi:10.1016/0092-8674(95)90541-3 · Cited by 2,367 · see citing works
Kaeberlein, M., McVey, M., & Guarente, L. (1999) · Genes & Development · doi:10.1101/gad.13.19.2570 · Cited by 2,253 · cited 2× · see citing works
“However, Sir2 remained as a largely overseen protein until Kaeberlein and collaborators demonstrated in 1999 how Sir2 could influence yeast replicative lifespan (Kaeberlein et al., 1999).”
BackgroundNegative 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
Sirtuins as regulators of metabolism and healthspan
Houtkooper, R. H., Pirinen, E., & Auwerx, J. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3293 · Cited by 2,008 · see citing works
Sirt1 promotes fat mobilization in white adipocytes by repressing PPAR-γ
Picard, F., Kurtev, M. V., Chung, N., Topark‐Ngarm, A., Senawong, T., de Oliveira, R. M., Leid, M. E., McBurney, M. W., & Guarente, L. (2004) · Nature · doi:10.1038/nature02583 · Cited by 1,943 · 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
Williamson, D., Lund, P., & Krebs, H. (1967) · Biochemical Journal · doi:10.1042/bj1030514 · Cited by 1,871 · see citing works
Leist, M., Single, B., Castoldi, A. F., Kühnle, S., & Nicotera, P. (1997) · The Journal of Experimental Medicine · doi:10.1084/jem.185.8.1481 · Cited by 1,871 · 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
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
Small molecule activators of SIRT1 as therapeutics for the treatment of type 2 diabetes
Milne, J. C., Lambert, P. D., Schenk, S., Carney, D. P., Smith, J. J., Gagne, D. J., Jin, L., Boss, O., Perni, R. B., Vu, C. B., et al. (2007) · Nature · doi:10.1038/nature06261 · Cited by 1,707 · see citing works
SIRT3 regulates mitochondrial fatty-acid oxidation by reversible enzyme deacetylation
Hirschey, M. D., Shimazu, T., Goetzman, E., Jing, E., Schwer, B., Lombard, D. B., Grueter, C. A., Harris, C., Biddinger, S., Ilkayeva, O. R., et al. (2010) · Nature · doi:10.1038/nature08778 · Cited by 1,687 · 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
Price, N. L., Gomes, A. P., Ling, A. J. Y., Duarte, F. V., Martin-Montalvo, A., North, B. J., Agarwal, B., Ye, L., Ramadori, G., Teodoro, J. S., et al. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.04.003 · Cited by 1,602 · see citing works
The Human Sir2 Ortholog, SIRT2, Is an NAD+-Dependent Tubulin Deacetylase
North, B. J., Marshall, B. L., Borra, M. T., Denu, J. M., & Verdin, E. M. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00038-8 · Cited by 1,542 · see citing works
Amé, J., Spenlehauer, C., & de MURCIA, G. (2004) · BioEssays · doi:10.1002/bies.20085 · Cited by 1,463 · see citing works
Sirt5 Is a NAD-Dependent Protein Lysine Demalonylase and Desuccinylase
Du, J., Zhou, Y., Su, X., Yu, J. J., Khan, S., Jiang, H., Kim, J., Woo, J., Kim, J. H., Choi, B. H., et al. (2011) · Science · doi:10.1126/science.1207861 · Cited by 1,429 · see citing works
Nakahata, Y., Kaluzova, M., Grimaldi, B., Sahar, S., Hirayama, J., Chen, D., Guarente, L. P., & Sassone-Corsi, P. (2008) · Cell · doi:10.1016/j.cell.2008.07.002 · Cited by 1,427 · see citing works
SIRT1 regulates circadian clock gene expression through PER2 deacetylation
Asher, G., Gatfield, D., Stratmann, M., Reinke, H., Dibner, C., Kreppel, F., Mostoslavsky, R., Alt, F. W., & Schibler, U. (2008) · Cell · doi:10.1016/j.cell.2008.06.050 · Cited by 1,376 · 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
Michishita, E., Park, J. Y., Burneskis, J. M., Barrett, J. C., & Horikawa, I. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-01-0033 · Cited by 1,364 · see citing works
Resveratrol Ameliorates Aging-Related Metabolic Phenotypes by Inhibiting cAMP Phosphodiesterases
Park, S. J., Ahmad, F., Philp, A., Baar, K., Williams, T., Luo, H., Ke, H., Rehmann, H., Taussig, R., Brown, A. L., et al. (2012) · Cell · doi:10.1016/j.cell.2012.01.017 · Cited by 1,352 · see citing works
Yoshino, J., Mills, K. F., Yoon, M. J., & Imai, S.-I. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.08.014 · Cited by 1,340 · see citing works
Calorie restriction reduces oxidative stress by SIRT3-mediated SOD2 activation
Qiu, X., Brown, K., Hirschey, M. D., Verdin, E., & Chen, D. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.11.015 · Cited by 1,310 · see citing works
Quinolinic Acid: An Endogenous Metabolite That Produces Axon-Sparing Lesions in Rat Brain
Schwarcz, R. M., Whetsell, W. O., & Mangano, R. M. (1983) · Science · doi:10.1126/science.6849138 · Cited by 1,269 · see citing works
Cantó, C., Houtkooper, R. H., Pirinen, E., Youn, D. Y., Oosterveer, M. H., Cen, Y., Fernandez-Marcos, P. J., Yamamoto, H., Andreux, P. A., Cettour-Rose, P., et al. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.04.022 · Cited by 1,238 · see citing works
Self-citationNew insights into the molecular and cellular functions of poly(ADP-ribose) and PARPs
Gibson, B. A., & Kraus, W. L. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3376 · Cited by 1,226 · see citing works
Mammalian Sir2 homolog SIRT3 regulates global mitochondrial lysine acetylation
Lombard, D. B., Alt, F. W., Cheng, H.-L., Bunkenborg, J., Streeper, R. S., Mostoslavsky, R., Kim, J., Yancopoulos, G., Valenzuela, D., Murphy, A., et al. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01636-07 · Cited by 1,216 · see citing works
Circadian Control of the NAD <sup>+</sup> Salvage Pathway by CLOCK-SIRT1
Nakahata, Y., Sahar, S., Astarita, G., Kaluzova, M., & Sassone-Corsi, P. (2009) · Science · doi:10.1126/science.1170803 · Cited by 1,198 · see citing works
DeFronzo, R. A., Gunnarsson, R., Björkman, O., Olsson, M., & Wahren, J. (1985) · Journal of Clinical Investigation · doi:10.1172/jci111938 · Cited by 1,167 · see citing works
Haigis, M. C., Mostoslavsky, R., Haigis, K. M., Fahie, K., Christodoulou, D. C., Murphy, A. J., Valenzuela, D. M., Yancopoulos, G. D., Karow, M., Blander, G., et al. (2006) · Cell · doi:10.1016/j.cell.2006.06.057 · Cited by 1,162 · see citing works
Someya, S., Yu, W., Hallows, W. C., Xu, J., Vann, J. M., Leeuwenburgh, C., Tanokura, M., Denu, J. M., & Prolla, T. A. (2010) · Cell · doi:10.1016/j.cell.2010.10.002 · Cited by 1,150 · see citing works
Sirt1 Regulates Aging and Resistance to Oxidative Stress in the Heart
Alcendor, R. R., Gao, S., Zhai, P., Zablocki, D., Holle, E., Yu, X., Tian, B., Wagner, T., Vatner, S. F., & Sadoshima, J. (2007) · Circulation Research · doi:10.1161/01.res.0000267723.65696.4a · Cited by 1,147 · see citing works
Circadian Clock Feedback Cycle Through NAMPT-Mediated NAD <sup>+</sup> Biosynthesis
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., et al. (2009) · Science · doi:10.1126/science.1171641 · Cited by 1,126 · see citing works
(ADP-ribose)n participates in DNA excision repair
Durkacz, B. W., Omidiji, O., Gray, D. A., & Shall, S. (1980) · Nature · doi:10.1038/283593a0 · Cited by 1,123 · see citing works
SIRT6 is a histone H3 lysine 9 deacetylase that modulates telomeric chromatin
Michishita, E., McCord, R. A., Berber, E., Kioi, M., Padilla-Nash, H., Damian, M., Cheung, P., Kusumoto, R., Kawahara, T. L. A., Barrett, J. C., et al. (2008) · Nature · doi:10.1038/nature06736 · Cited by 1,111 · see citing works
Developmental defects and p53 hyperacetylation in Sir2 homolog (SIRT1)-deficient mice
Cheng, H.-L., Mostoslavsky, R., Saito, S., Manis, J. P., Gu, Y., Patel, P., Bronson, R., Appella, E., Alt, F. W., & Chua, K. F. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1934713100 · Cited by 1,095 · see citing works
Mechanism of Human SIRT1 Activation by Resveratrol
Borra, M. T., Smith, B. C., & Denu, J. M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501250200 · Cited by 1,065 · see citing works
The sirtuin SIRT6 regulates lifespan in male mice
Kanfi, Y., Naiman, S., Amir, G., Peshti, V., Zinman, G., Nahum, L., Bar-Joseph, Z., & Cohen, H. Y. (2012) · Nature · doi:10.1038/nature10815 · Cited by 1,059 · see citing works
Requirement of poly(ADP-ribose) polymerase in recovery from DNA damage in mice and in cells
Murcia, J. M., Niedergang, C., Trucco, C., Ricoul, M., Dutrillaux, B., Mark, M. P., Oliver, F. J., Masson, M., Dierich, A., LeMeur, M., et al. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.14.7303 · Cited by 1,058 · 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
Tankyrase, a Poly(ADP-Ribose) Polymerase at Human Telomeres
Smith, S. H., Giriat, I., Schmitt, A., & de Lange, T. (1998) · Science · doi:10.1126/science.282.5393.1484 · Cited by 1,006 · see citing works
The Histone Deacetylase Sirt6 Regulates Glucose Homeostasis via Hif1α
Zhong, L., D'Urso, A., Toiber, D., Sebastian, C., Henry, R. E., Vadysirisack, D. D., Guimaraes, A., Marinelli, B., Wikstrom, J. D., Nir, T., et al. (2010) · Cell · doi:10.1016/j.cell.2009.12.041 · Cited by 1,001 · see citing works
Nutrient-Sensitive Mitochondrial NAD+ Levels Dictate Cell Survival
Yang, H., Yang, T., Baur, J. A., Perez, E., Matsui, T., Carmona, J. J., Lamming, D. W., Souza-Pinto, N. C., Bohr, V. A., Rosenzweig, A., et al. (2007) · Cell · doi:10.1016/j.cell.2007.07.035 · Cited by 950 · see citing works
Self-citationSirt1 protects against high-fat diet-induced metabolic damage
Pfluger, P. T., Herranz, D., Velasco-Miguel, S., Serrano, M., & Tschöp, M. H. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0802917105 · Cited by 928 · see citing works
Cantó, C., Jiang, L. Q., Deshmukh, A. S., Mataki, C., Coste, A., Lagouge, M., Zierath, J. R., & Auwerx, J. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.02.006 · Cited by 921 · see citing works
Self-citationSRT1720, SRT2183, SRT1460, and resveratrol are not direct activators of SIRT1
Pacholec, M., Bleasdale, J. E., Chrunyk, B., Cunningham, D., Flynn, D., Garofalo, R. S., Griffith, D., Griffor, M., Loulakis, P., Pabst, B., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.088682 · Cited by 915 · see citing works
Nampt/PBEF/Visfatin Regulates Insulin Secretion in β Cells as a Systemic NAD Biosynthetic Enzyme
Revollo, J. R., Körner, A., Mills, K. F., Satoh, A., Wang, T., Garten, A., Dasgupta, B., Sasaki, Y., Wolberger, C., Townsend, R. R., et al. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.09.003 · Cited by 911 · see citing works
Poly(ADP-ribose) polymerase is a mediator of necrotic cell death by ATP depletion
Ha, H. C., & Snyder, S. H. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.24.13978 · Cited by 904 · see citing works
The secret life of NAD+: an old metabolite controlling new metabolic signaling pathways
Houtkooper, R. H., Cantó, C., Wanders, R. J., & Auwerx, J. (2010) · Endocrine Reviews · doi:10.1210/er.2009-0026 · Cited by 899 · see citing works
Self-citationPoly(ADP-ribose) polymerase and the therapeutic effects of its inhibitors
Jagtap, P. G., & Szabó, C. (2005) · Nature Reviews Drug Discovery · doi:10.1038/nrd1718 · Cited by 896 · see citing works
SIRT6 Promotes DNA Repair Under Stress by Activating PARP1
Mao, Z., Hine, C., Tian, X., Van Meter, M., Au, M., Vaidya, A., Seluanov, A., & Gorbunova, V. (2011) · Science · doi:10.1126/science.1202723 · Cited by 867 · see citing works
SIRT1 redistribution on chromatin promotes genomic stability but alters gene expression during aging
Oberdoerffer, P., Michan, S., McVay, M., Mostoslavsky, R., Vann, J., Park, S.-K., Hartlerode, A., Stegmuller, J., Hafner, A., Loerch, P., et al. (2008) · Cell · doi:10.1016/j.cell.2008.10.025 · Cited by 852 · see citing works
PARP-1 inhibition increases mitochondrial metabolism through SIRT1 activation
Bai, P., Cantó, C., Oudart, H., Brunyánszki, A., Cen, Y., Thomas, C., Yamamoto, H., Huber, A., Kiss, B., Houtkooper, R. H., et al. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.03.004 · Cited by 837 · see citing works
Self-citationEtiology of Insulin Resistance
Petersen, K. F., & Shulman, G. I. (2006) · The American Journal of Medicine · doi:10.1016/j.amjmed.2006.01.009 · Cited by 825 · see citing works
SIRT1 Modulation of the Acetylation Status, Cytosolic Localization, and Activity of LKB1
Lan, F., Cacicedo, J. M., Ruderman, N., & Ido, Y. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m805711200 · Cited by 825 · see citing works
Fulco, M., Cen, Y., Zhao, P., Hoffman, E. P., McBurney, M. W., Sauve, A. A., & Sartorelli, V. (2008) · Developmental Cell · doi:10.1016/j.devcel.2008.02.004 · Cited by 821 · see citing works
Self-citationToward a unified nomenclature for mammalian ADP-ribosyltransferases
Hottiger, M. O., Hassa, P. O., Lüscher, B., Schuler, H., & Koch‐Nolte, F. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2009.12.003 · Cited by 814 · see citing works
Brown Remodeling of White Adipose Tissue by SirT1-Dependent Deacetylation of Pparγ
Qiang, L., Wang, L., Kon, N., Zhao, W., Lee, S., Zhang, Y., ROSENBAUM, M. S., Zhao, Y., Gu, W. J., Farmer, S. R., et al. (2012) · Cell · doi:10.1016/j.cell.2012.06.027 · Cited by 802 · see citing works
PUMA-G and HM74 are receptors for nicotinic acid and mediate its anti-lipolytic effect
Tunaru, S., Kero, J. T., Schaub, A., Wufka, C., Blaukat, A., Pfeffer, K., & Offermanns, S. (2003) · Nature Medicine · doi:10.1038/nm824 · Cited by 794 · see citing works
Hirschey, M. D., Shimazu, T., Jing, E., Grueter, C. A., Collins, A. M., Aouizerat, B., Stančáková, A., Goetzman, E., Lam, M. M., Schwer, B., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.07.019 · Cited by 787 · see citing works
SIRT5 deacetylates carbamoyl phosphate synthetase 1 and regulates the urea cycle
Nakagawa, T., Lomb, D. J., Haigis, M. C., & Guarente, L. (2009) · Cell · doi:10.1016/j.cell.2009.02.026 · Cited by 787 · see citing works
Kim, H.-S., Patel, K., Muldoon-Jacobs, K., Bisht, K. S., Aykin-Burns, N., Pennington, J. D., van der Meer, R., Nguyen, P., Savage, J., Owens, K. M., et al. (2010) · Cancer Cell · doi:10.1016/j.ccr.2009.11.023 · Cited by 785 · see citing works
Nucleocytoplasmic Shuttling of the NAD+-dependent Histone Deacetylase SIRT1*
Tanno, M., Sakamoto, J., Miura, T., Shimamoto, K., & Horio, Y. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m609554200 · Cited by 784 · see citing works
SIRT1 Regulates Hepatocyte Lipid Metabolism through Activating AMP-activated Protein Kinase
Hou, X., Xu, S., Maitland-Toolan, K. A., Sato, K., Jiang, B., Ido, Y., Lan, F., Walsh, K., Wierzbicki, M., Verbeuren, T. J., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802187200 · Cited by 778 · see citing works
Poly(ADP-Ribose) in the Cellular Response to DNA Damage
Berger, N. A. (1985) · Radiation Research · doi:10.2307/3576299 · Cited by 777 · see citing works
Mice lacking ADPRT and poly(ADP-ribosyl)ation develop normally but are susceptible to skin disease.Preprint
Wang, Z. Q., Auer, B., Stingl, L., Berghammer, H., Haidacher, D., Schweiger, M. R., & Wagner, E. F. (1995) · Genes & Development · doi:10.1101/gad.9.5.509 · Cited by 774 · 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
Self-citationBieganowski, P., & Brenner, C. (2004) · Cell · doi:10.1016/s0092-8674(04)00416-7 · Cited by 750 · see citing works
Substrate-specific activation of sirtuins by resveratrol
Kaeberlein, M., McDonagh, T., Heltweg, B., Hixon, J., Westman, E. A., Caldwell, S. D., Napper, A., Curtis, R., DiStefano, P. S., Fields, S., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500655200 · Cited by 745 · see citing works
PARP-2, A Novel Mammalian DNA Damage-dependent Poly(ADP-ribose) Polymerase
Amé, J., Rolli, V., Schreiber, V., Niedergang, C., Apiou, F., Decker, P., Muller, S., Höger, T. H., Murcia, J. M., & de MURCIA, G. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.25.17860 · Cited by 744 · see citing works
Influence of nicotinic acid on serum cholesterol in man
Altschul, R., Hoffer, A., & Stephen, J. D. (1955) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(55)90070-9 · Cited by 726 · see citing works
Resveratrol stimulates AMP kinase activity in neurons
Dasgupta, B., & Milbrandt, J. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0610068104 · Cited by 723 · see citing works
Feige, J. N., Lagouge, M., Canto, C., Strehle, A., Houten, S. M., Milne, J. C., Lambert, P. D., Mataki, C., Elliott, P. J., & Auwerx, J. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.08.017 · Cited by 719 · see citing works
Sir2 links chromatin silencing, metabolism, and agingPreprint
Guarente, L. (2000) · Genes & Development · doi:10.1101/gad.14.9.1021 · Cited by 718 · see citing works
Kong, X., Wang, R., Xue, Y., Liu, X., Zhang, H., Chen, Y., Fang, F., & Chang, Y. (2010) · PLoS ONE · doi:10.1371/journal.pone.0011707 · Cited by 718 · see citing works
Sirt1 Regulates Insulin Secretion by Repressing UCP2 in Pancreatic β Cells
Bordone, L., Motta, M. C., Picard, F., Robinson, A., Jhala, U. S., Apfeld, J., McDonagh, T., Lemieux, M., McBurney, M., Szilvasi, A., et al. (2005) · PLoS Biology · doi:10.1371/journal.pbio.0040031 · Cited by 715 · see citing works
Bogan, K. L., & Brenner, C. (2008) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.28.061807.155443 · Cited by 707 · see citing works
Schreiber, V., Amé, J., Dollé, P., Schultz, I., Rinaldi, B., Fraulob, V., Murcia, J. M., & de MURCIA, G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202390200 · Cited by 706 · see citing works
Nuclear ADP-Ribosylation Reactions in Mammalian Cells: Where Are We Today and Where Are We Going?
Hassa, P. O., Haenni, S. S., Elser, M., & Hottiger, M. O. (2006) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00040-05 · Cited by 682 · see citing works
Nutrient Availability Regulates SIRT1 Through a Forkhead-Dependent Pathway
Nemoto, S., Fergusson, M. M., & Finkel, T. (2004) · Science · doi:10.1126/science.1101731 · Cited by 671 · see citing works
Structural Basis for DNA Damage–Dependent Poly(ADP-ribosyl)ation by Human PARP-1
Langelier, M.-F., Planck, J. L., Roy, S., & Pascal, J. M. (2012) · Science · doi:10.1126/science.1216338 · Cited by 669 · see citing works
Chambon, P., Weill, J. D., & Mandel, P. (1963) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(63)90024-x · Cited by 654 · see citing works
Regulation of SIRT1 in cellular functions: Role of polyphenols
Chung, S., Yao, H., Caito, S. W., Hwang, J., Arunachalam, G., & Rahman, I. (2010) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2010.05.003 · Cited by 651 · 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
AMP-activated protein kinase-deficient mice are resistant to the metabolic effects of resveratrol
Um, J.-H., Park, S.-J., Kang, H., Yang, S., Foretz, M., McBurney, M. W., Kim, M. K., Viollet, B., & Chung, J. H. (2010) · Diabetes · doi:10.2337/db09-0482 · Cited by 647 · see citing works
Vakhrusheva, O., Smolka, C., Gajawada, P., Sawa Kostin, D., Boettger, T., Kubin, T., Braun, T. W., & Bober, E. (2008) · Circulation Research · doi:10.1161/circresaha.107.164558 · Cited by 639 · see citing works
SirT1 Gain of Function Increases Energy Efficiency and Prevents Diabetes in Mice
Banks, A. S., Kon, N., Knight, C. M., Matsumoto, M., Juárez, R. G., Rossetti, L., Gu, W. J., & Accili, D. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.08.014 · Cited by 636 · see citing works
Moynihan, K. A., Grimm, A. A., Plueger, M. M., Bernal‐Mizrachi, E., Ford, E. L., CRAS-MÉNEUR, C. M. H., Permutt, M. A., & Imai, S. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.07.001 · Cited by 630 · see citing works
Murcia, J. M., Ricoul, M., Tartier, L., Niedergang, C., Huber, A., Dantzer, F., Schreiber, V., Amé, J., Dierich, A., LeMeur, M., et al. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg206 · Cited by 629 · 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
Qin, W., Yang, T., Ho, L., Zhao, Z., Wang, J., Chen, L., Zhao, W., Thiyagarajan, M., MacGrogan, D., Rodgers, J. T., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602909200 · Cited by 626 · see citing works
Self-citationAbsence of effects of Sir2 overexpression on lifespan in C. elegans and Drosophila
Burnett, C., Valentini, S., Cabreiro, F., Goss, M., Somogyvári, M., Piper, M. D., Hoddinott, M., Sutphin, G. L., Leko, V., McElwee, J. J., et al. (2011) · Nature · doi:10.1038/nature10296 · Cited by 624 · see citing works
SIRT7 links H3K18 deacetylation to maintenance of oncogenic transformation
Barber, M. F., Michishita-Kioi, E., Xi, Y., Tasselli, L., Kioi, M., Moqtaderi, Z., Tennen, R. I., Paredes, S., Young, N. L., Chen, K., et al. (2012) · Nature · doi:10.1038/nature11043 · Cited by 621 · see citing works
The Mammalian SIR2α Protein Has a Role in Embryogenesis and Gametogenesis
McBurney, M. W., Yang, X., Jardine, K., Hixon, M., Boekelheide, K., Webb, J. R., Lansdorp, P. M., & Lemieux, M. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.1.38-54.2003 · Cited by 611 · see citing works
Schwer, B., North, B. J., Frye, R. A., Ott, M., & Verdin, E. M. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200205057 · Cited by 599 · see citing works
Oliver, F. J., Murcia, J. M., Nacci, C., Decker, P., Andriantsitohaina, R., Muller, S., de la Rubia, G., Stoclet, J., & de MURCIA, G. (1999) · The EMBO Journal · doi:10.1093/emboj/18.16.4446 · Cited by 583 · see citing works
Tissue-specific regulation of SIRT1 by calorie restriction
Chen, D., Bruno, J., Easlon, E., Lin, S.-J., Cheng, H.-L., Alt, F. W., & Guarente, L. (2008) · Genes & Development · doi:10.1101/gad.1650608 · Cited by 567 · see citing works
Nitric oxide, cell bioenergetics and neurodegeneration
Moncada, S., & Bolaños, J. P. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03988.x · Cited by 556 · see citing works
The role of FoxO in the regulation of metabolism
Gross, D. N., van den Heuvel, A. P. J., & Birnbaum, M. J. (2008) · Oncogene · doi:10.1038/onc.2008.25 · Cited by 555 · see citing works
Fasting-dependent glucose and lipid metabolic response through hepatic sirtuin 1
Rodgers, J. T., & Puigserver, P. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0702509104 · Cited by 549 · see citing works
Mouse Sir2 Homolog SIRT6 Is a Nuclear ADP-ribosyltransferase
Liszt, G., Ford, E., Kurtev, M., & Guarente, L. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413296200 · Cited by 548 · see citing works
Age-Associated Changes In Oxidative Stress and NAD+ Metabolism In Human Tissue
Massudi, H., Grant, R., Braidy, N., Guest, J., Farnsworth, B., & Guillemin, G. J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0042357 · Cited by 545 · cited 6× · see citing works
“in aging (Braidy et al., 2011; Massudi et al., 2012)) that presumably contributes to these pathologies.”
BackgroundInfluentialMolecular Identification of High and Low Affinity Receptors for Nicotinic Acid
Wise, A., Foord, S. M., Fraser, N. J., Barnes, A. A., Elshourbagy, N. A., Eilert, M. M., Ignar, D. M., Murdock, P. R., Steplewski, K. M., Green, A. R., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210695200 · Cited by 540 · see citing works
Honjo, T., Nishizuka, Y., Hayaishi, O., & Kato, I. (1968) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)93347-8 · Cited by 537 · see citing works
Gale, E. A. (2004) · The Lancet · doi:10.1016/s0140-6736(04)15786-3 · Cited by 534 · see citing works
Novel inhibitors of poly(ADP-ribose) synthetase
Purnell, M. R., & WHISH, W. J. D. (1980) · Biochemical Journal · doi:10.1042/bj1850775 · Cited by 529 · see citing works
Kynurenine 3-Monooxygenase Inhibition in Blood Ameliorates Neurodegeneration
Zwilling, D., Huang, S., Sathyasaikumar, K. V., Notarangelo, F. M., Guidetti, P., Wu, H., Lee, J. H., Truong, J. K., Andrews-Zwilling, Y. S., Hsieh, E., et al. (2011) · Cell · doi:10.1016/j.cell.2011.05.020 · Cited by 519 · see citing works
(2010) · doi:10.1016/j.cmet.2010.06.009 · Cited by 512 · see citing works
Base Excision Repair Is Impaired in Mammalian Cells Lacking Poly(ADP-ribose) Polymerase-1
Dantzer, F., de la Rubia, G., Murcia, J. M., Hostomský, Z., de MURCIA, G., & Schreiber, V. (2000) · Biochemistry · doi:10.1021/bi0003442 · Cited by 505 · see citing works
DBC1 is a negative regulator of SIRT1
Kim, J., Chen, J., & Lou, Z. (2008) · Nature · doi:10.1038/nature06500 · Cited by 503 · see citing works
The macro domain is an ADP‐ribose binding module
Karras, G. I., Kustatscher, G., Buhecha, H. R., Allen, M. D., Pugieux, C., Sait, F., Bycroft, M., & Ladurner, A. G. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600664 · Cited by 502 · see citing works
The diverse roles and clinical relevance of PARPs in DNA damage repair: Current state of the art
Vos, M. D., Schreiber, V., & Dantzer, F. (2012) · Biochemical Pharmacology · doi:10.1016/j.bcp.2012.03.018 · Cited by 491 · see citing works
SIRT2 Regulates Adipocyte Differentiation through FoxO1 Acetylation/Deacetylation
Jing, E., Gesta, S., & Kahn, C. R. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.07.003 · Cited by 490 · see citing works
Benjamin, R. C., & Gill, D. M. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)70491-8 · Cited by 489 · see citing works
Diet and exercise signals regulate SIRT3 and activate AMPK and PGC-1α in skeletal muscle
Palacios, O. M., Carmona, J. J., Michan, S., Chen, K. Y., Manabe, Y., III, J. L. W., Goodyear, L. J., & Tong, Q. (2009) · Aging · doi:10.18632/aging.100075 · Cited by 487 · see citing works
Shimazu, T., Hirschey, M. D., Hua, L., Dittenhafer-Reed, K. E., Schwer, B., Lombard, D. B., Li, Y., Bunkenborg, J., Alt, F. W., Denu, J. M., et al. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.11.003 · Cited by 484 · see citing works
Endogenous Nmnat2 Is an Essential Survival Factor for Maintenance of Healthy Axons
Gilley, J., & Coleman, M. P. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000300 · Cited by 472 · see citing works
Negative regulation of the deacetylase SIRT1 by DBC1
Zhao, W., Kruse, J.-P., Tang, Y., Jung, S. Y., Qin, J., & Gu, W. J. (2008) · Nature · doi:10.1038/nature06515 · Cited by 464 · see citing works
Family-wide chemical profiling and structural analysis of PARP and tankyrase inhibitors
Wahlberg, E., Karlberg, T., Kouznetsova, E., Markova, N., Macchiarulo, A., Thorsell, A. G., Pol, E., Frostell, Å., Ekblad, T., Öncü, D., et al. (2012) · Nature Biotechnology · doi:10.1038/nbt.2121 · Cited by 460 · see citing works
Bell, E. L., Emerling, B. M., Ricoult, S. J. H., & Guarente, L. (2011) · Oncogene · doi:10.1038/onc.2011.37 · Cited by 440 · see citing works
Targeting Sirtuin 1 to Improve Metabolism: All You Need Is NAD+?
Cantó, C., & Auwerx, J. (2012) · Pharmacological Reviews · doi:10.1124/pr.110.003905 · Cited by 433 · see citing works
Self-citationAMP-activated protein kinase and its downstream transcriptional pathways
Cantó, C., & Auwerx, J. (2010) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-010-0454-z · Cited by 421 · see citing works
Self-citationA complex barcode underlies the heterogeneous response of p53 to stress
Murray-Zmijewski, F., Slee, E. A., & Lu, X. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2451 · Cited by 420 · see citing works
Jiang, W., Wang, S., Xiao, M., Lin, Y., Zhou, L., Lei, Q., Xiong, Y., Guan, K., & Zhao, S. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.04.028 · Cited by 415 · see citing works
Epstein, W., & Beckwith, J. R. (1968) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.37.070168.002211 · Cited by 413 · see citing works
Kraus, W. L. (2008) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2008.03.006 · Cited by 409 · see citing works
Biosynthesis of Diphosphopyridine Nucleotide
Preiss, J., & Handler, P. (1958) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)64790-8 · Cited by 408 · see citing works
Biosynthesis of Diphosphopyridine Nucleotide
Preiss, J., & Handler, P. (1958) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)64789-1 · Cited by 403 · see citing works
Caloric restriction, SIRT1 and longevity
Cantó, C., & Auwerx, J. (2009) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2009.03.008 · Cited by 395 · see citing works
Self-citationPillai, 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
Reciprocal Binding of PARP-1 and Histone H1 at Promoters Specifies Transcriptional Outcomes
Krishnakumar, R., Gamble, M. J., Frizzell, K. M., Berrocal, J. G., Kininis, M., & Kraus, W. L. (2008) · Science · doi:10.1126/science.1149250 · Cited by 382 · see citing works
SIRT2 regulates NF-κB-dependent gene expression through deacetylation of p65 Lys310
Rothgiesser, K., Erener, S., Waibel, S., Lüscher, B., & Hottiger, M. O. (2010) · Journal of Cell Science · doi:10.1242/jcs.073783 · Cited by 376 · see citing works
Evolution of Poly(ADP-ribose) Polymerase-1 (PARP-1) Inhibitors. From Concept to Clinic
Ferraris, D. V. (2010) · Journal of Medicinal Chemistry · doi:10.1021/jm100012m · Cited by 375 · see citing works
Burkart, V., Wang, Z., Radons, J., Heller, B., Herceg, Z., Stingl, L., Wagner, E. F., & Kolb, H. (1999) · Nature Medicine · doi:10.1038/6535 · Cited by 371 · see citing works
Han, M., Song, E.-K., Guo, Y., Ou, X., Mantel, C., & Broxmeyer, H. E. (2008) · Cell stem cell · doi:10.1016/j.stem.2008.01.002 · Cited by 368 · see citing works
Mitochondrial biogenesis and healthy aging
López-Lluch, G., Irusta, P. M., Navas, P., & de Cabo, R. (2008) · Experimental Gerontology · doi:10.1016/j.exger.2008.06.014 · Cited by 364 · see citing works
Role of the Peroxynitrite-Poly(ADP-Ribose) Polymerase Pathway in Human Disease
Pacher, P., & Szabó, C. (2008) · American Journal Of Pathology · doi:10.2353/ajpath.2008.080019 · Cited by 364 · see citing works
GPR109A (PUMA-G/HM74A) mediates nicotinic acid–induced flushing
Benyó, Z., Gille, A., Kero, J. T., Csiky, M., Suchánková, M. C., Nüsing, R. M., Moers, A., Pfeffer, K., & Offermanns, S. (2005) · Journal of Clinical Investigation · doi:10.1172/jci23626 · Cited by 344 · see citing works
Substrate-Assisted Catalysis by PARP10 Limits Its Activity to Mono-ADP-Ribosylation
Kleine, H., Poręba, E., Leśniewicz, K., Hassa, P. O., Hottiger, M. O., Litchfield, D. W., Shilton, B. H., & Lüscher, B. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.08.009 · Cited by 340 · see citing works
Poly(ADP-ribose) polymerase 1 participates in the phase entrainment of circadian clocks to feeding
Asher, G., Reinke, H., Altmeyer, M., Gutierrez-Arcelus, M., Hottiger, M. O., & Schibler, U. (2010) · Cell · doi:10.1016/j.cell.2010.08.016 · Cited by 340 · see citing works
SIRT2 inhibition achieves neuroprotection by decreasing sterol biosynthesis
Luthi‐Carter, R., Taylor, D. M., Pallos, J., Lambert, E., Amore, A. M., Parker, J. A., Moffitt, H., Smith, D. L., Runne, H., Gökçe, Ö., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1002924107 · Cited by 338 · see citing works
PARP-3 and APLF Function Together to Accelerate Nonhomologous End-Joining
Rulten, S. L., Fisher, A. E. O., Robert, I., Zuma, M. C., Rouleau, M., Ju, L., Poirier, G. G., Reina‐San‐Martin, B., & Caldecott, K. W. (2011) · Molecular Cell · doi:10.1016/j.molcel.2010.12.006 · 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
Altmeyer, M., Messner, S., Hassa, P. O., Fey, M., & Hottiger, M. O. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp229 · Cited by 325 · see citing works
SIRT4 Regulates Fatty Acid Oxidation and Mitochondrial Gene Expression in Liver and Muscle Cells
Nasrin, N., Wu, X.-P., Fortier, E., Feng, Y., Bare, O., Chen, S., Ren, X., Wu, Z., Streeper, R. S., & Bordone, L. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.124164 · Cited by 323 · see citing works
Gerhart‐Hines, Z., Dominy, J. E., Blättler, S. M., Jedrychowski, M. P., Banks, A. S., Lim, J.-H., Chim, H., Gygi, S. P., & Puigserver, P. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.12.005 · Cited by 323 · see citing works
Mortusewicz, O., Amé, J., Schreiber, V., & Leonhardt, H. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm933 · Cited by 321 · see citing works
The role of PARP in DNA repair and its therapeutic exploitation
Javle, M. M., & Curtin, N. J. (2011) · British Journal of Cancer · doi:10.1038/bjc.2011.382 · Cited by 320 · see citing works
Molecular identification of nicotinic acid receptor
Soga, T., Kamohara, M., Takasaki, J., Matsumoto, S., Saito, T., Ohishi, T., Hiyama, H., Matsuo, A., Matsushime, H., & Furuichi, K. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)00342-5 · Cited by 316 · see citing works
The Role of PARP-1 and PARP-2 Enzymes in Metabolic Regulation and Disease
Bai, P., & Cantó, C. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.06.016 · Cited by 312 · see citing works
Self-citationStructure and Biochemical Functions of SIRT6
Pan, P. W., Feldman, J. L., Devries, M., Dong, A., Edwards, A. M., & Denu, J. M. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.218990 · Cited by 311 · see citing works
SIRT6 protects against pathological damage caused by diet‐induced obesity
Kanfi, Y., Peshti, V., Gil, R., Naiman, S., Nahum, L., Levin, E., Kronfeld‐Schor, N., & Cohen, H. Y. (2010) · Aging Cell · doi:10.1111/j.1474-9726.2009.00544.x · 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
Hassa, P. O., Haenni, S. S., Buerki, C., Meier, N. I., Lane, W. S., Owen, H., Gersbach, M., Imhof, R., & Hottiger, M. O. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m507553200 · Cited by 306 · see citing works
Rajamohan, S. B., Pillai, V. B., Gupta, M., Sundaresan, N. R., Birukov, K. G., Samant, S. A., Hottiger, M. O., & Gupta, M. P. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00121-09 · Cited by 303 · see citing works
NAD+ and Vitamin B3: From Metabolism to Therapies
Sauve, A. A. (2007) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.107.120758 · Cited by 303 · see citing works
Self-citationPoly(ADP-ribosyl)ation regulates CTCF-dependent chromatin insulation
Yu, W., Ginjala, V., Pant, V., Chernukhin, I. V., Whitehead, J., Docquier, F., Farrar, D., Tavoosidana, G., Mukhopadhyay, R., Kanduri, C., et al. (2004) · Nature Genetics · doi:10.1038/ng1426 · Cited by 298 · see citing works
Skeletal muscle NAMPT is induced by exercise in humans
Costford, S. R., Bajpeyi, S., Pasarica, M., Albarado, D. C., Thomas, S. C., Xie, H., Church, T. S., Jubrias, S. A., Conley, K. E., & Smith, S. R. (2009) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00318.2009 · Cited by 297 · see citing works
Caito, S. W., Rajendrasozhan, S., Cook, S., Chung, S., Yao, H., Friedman, A. E., Brookes, P. S., & Rahman, I. (2010) · The FASEB Journal · doi:10.1096/fj.09-151308 · Cited by 296 · 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
Cloning and characterization of four SIR genes of Saccharomyces cerevisiae.
Ivy, J. M., Klar, A. J. S., & Hicks, J. B. (1986) · Molecular and Cellular Biology · doi:10.1128/mcb.6.2.688 · Cited by 294 · see citing works
Nakagawa, T., & Guarente, L. (2011) · Journal of Cell Science · doi:10.1242/jcs.081067 · Cited by 289 · see citing works
Calorie Restriction: Is AMPK a Key Sensor and Effector
Cantó, C., & Auwerx, J. (2011) · Physiology · doi:10.1152/physiol.00010.2011 · Cited by 282 · see citing works
Self-citationPacher, P., Liaudet, L., Bai, P., Mabley, J. G., Kaminski, P. M., Virág, L., Deb, A., Szabó, É., Ungvari, Z. I., Wolin, M. S., et al. (2003) · Circulation · doi:10.1161/01.cir.0000048192.52098.dd · Cited by 279 · see citing works
Self-citationSKIDMORE, C. J., DAVIES, M. I., Goodwin, P. M., Halldórsson, H., Lewis, P., Shall, S., & ZIA'EE, A. (1979) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1979.tb04225.x · Cited by 278 · see citing works
Boehler, C., Gauthier, L., Mortusewicz, O., Biard, D. S. F., Saliou, J., Bresson, A., Cianférani, S., Smith, S. H., Schreiber, V., Boussin, F. D., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1016574108 · Cited by 277 · see citing works
Inhibition of Mitochondrial ATP Generation by Nitric Oxide Switches Apoptosis to Necrosis
Leist, M., Single, B., Naumann, H., Fava, E., Simon, B., Kühnle, S., & Nicotera, P. (1999) · Experimental Cell Research · doi:10.1006/excr.1999.4514 · Cited by 275 · see citing works
Brookins-Danz, E. D., Skramsted, J., Henry, N., Bennett, J. A., & Keller, R. S. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.03.011 · Cited by 266 · see citing works
Szabó, C., Virág, L., Cuzzocrea, S., Scott, G. S., Hake, P. W., O’Connor, M., Zingarelli, B., Salzman, A. L., & Kun, E. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.7.3867 · Cited by 262 · see citing works
Hiratsuka, M., Inoue, T., Toda, T., Kimura, N., Shirayoshi, Y., Kamitani, H., Watanabe, T., Ohama, E., Tahimic, C. G. T., Kurimasa, A., et al. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2003.08.029 · Cited by 261 · see citing works
In silico characterization of the family of PARP-like poly(ADP-ribosyl)transferases (pARTs)
Otto, H., Reche, P. A., Bazán, F., Dittmar, K., Haag, F., & Koch‐Nolte, F. (2005) · BMC Genomics · doi:10.1186/1471-2164-6-139 · Cited by 259 · see citing works
SIRT3, a pivotal actor in mitochondrial functions: metabolism, cell death and aging
Giralt, A., & Villarroya, F. (2012) · Biochemical Journal · doi:10.1042/bj20120030 · Cited by 253 · see citing works
Effects of resveratrol on the rat brain respiratory chain.
Zini, R., Morin, C., Bertelli, A., Bertelli, A., & Tillement, J. P. (1999) · PubMed · Cited by 252 · see citing works
PARP-2 Regulates SIRT1 Expression and Whole-Body Energy Expenditure
Bai, P., Cantó, C., Brunyánszki, A., Huber, A., Szántó, M., Cen, Y., Yamamoto, H., Houten, S. M., Kiss, B., Oudart, H., et al. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.03.013 · Cited by 250 · see citing works
Self-citationLiu, D., Gharavi, R. B., PITTA, M. G. R., Gleichmann, M., & Mattson, M. P. (2009) · NeuroMolecular Medicine · doi:10.1007/s12017-009-8058-1 · Cited by 248 · see citing works
Virág, L., Salzman, A. L., & Szabó, C. (1998) · The Journal of Immunology · doi:10.4049/jimmunol.161.7.3753 · Cited by 248 · see citing works
Structure of the catalytic fragment of poly(AD-ribose) polymerase from chicken.
Ruf, A., Murcia, J. M., de MURCIA, G., & Schulz, G. E. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.15.7481 · Cited by 243 · see citing works
Inhibitors of Poly(Adenosine Diphosphate-Ribose) Synthesis: Effect on Other Metabolic Processes
Milam, K. M., & Cleaver, J. E. (1984) · Science · doi:10.1126/science.6420886 · Cited by 241 · see citing works
Mechanism of Nicotinamide Inhibition and Transglycosidation by Sir2 Histone/Protein Deacetylases
Jackson, M. D., Schmidt, M. T., Oppenheimer, N. J., & Denu, J. M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306552200 · Cited by 238 · see citing works
Hasegawa, K., Wakino, S., Yoshioka, K., Tatematsu, S., Hara, Y., Minakuchi, H., Washida, N., Tokuyama, H., Hayashi, K., & Itoh, H. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.04.176 · Cited by 235 · see citing works
A c-Myc–SIRT1 feedback loop regulates cell growth and transformation
Yuan, J., Minter‐Dykhouse, K., & Lou, Z. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200809167 · Cited by 232 · see citing works
Kurnasov, O. V., Goral, V. N., Colabroy, K. L., Gerdes, S., Anantha, S., Osterman, A. L., & Begley, T. P. (2003) · Chemistry & Biology · doi:10.1016/j.chembiol.2003.11.011 · Cited by 230 · see citing works
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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
Self-citationNAD+ metabolism and its roles in cellular processes during ageing
Covarrubias, A. J., Perrone, R., Grozio, A., & Verdin, E. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-00313-x · Cited by 1,617 · see citing works
The sirtuin family in health and disease
Wu, Q., Zhang, T., Chen, H., Yu, X., Lv, J.-L., Liu, Y., Liu, Y., Zheng, G., Zhao, J.-Q., Wei, Y., et al. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01257-8 · Cited by 891 · see citing works
NAD + metabolism: Bioenergetics, signaling and manipulation for therapy
Yang, Y. J., & Sauve, A. A. (2016) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2016.06.014 · Cited by 488 · see citing works
Self-citationHou, Y., Lautrup, S., Cordonnier, S., Wang, Y., Croteau, D. L., Zavala, E., Zhang, Y., Moritoh, K., O’Connell, J. F., Baptiste, B. A., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1718819115 · Cited by 472 · see citing works
CD38-Mediated Immunosuppression as a Mechanism of Tumor Cell Escape from PD-1/PD-L1 Blockade
Chen, L., Diao, L., Yang, Y., Yi, X., Rodriguez, B. L., Li, Y., Villalobos, P. A., Cascone, T., Liu, X., Tan, L., et al. (2018) · Cancer Discovery · doi:10.1158/2159-8290.cd-17-1033 · Cited by 462 · see citing works
Biology of Poly(ADP-Ribose) Polymerases: The Factotums of Cell Maintenance
Bai, P. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.01.034 · Cited by 445 · see citing works
Self-citationSirtuins in Renal Health and Disease
Morigi, M., Perico, L., & Benigni, A. (2018) · Journal of the American Society of Nephrology · doi:10.1681/asn.2017111218 · Cited by 359 · see citing works
Repairing mitochondrial dysfunction in disease
Sorrentino, V., Menzies, K. J., & Auwerx, J. (2018) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010716-104908 · Cited by 337 · see citing works
Protein acetylation in metabolism – metabolites and cofactors
Menzies, K. J., Zhang, H., Katsyuba, E., & Auwerx, J. (2016) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2015.181 · Cited by 331 · see citing works
Sirtuins: guardians of mammalian healthspan
Giblin, W., Skinner, M. E., & Lombard, D. B. (2014) · Trends in Genetics · doi:10.1016/j.tig.2014.04.007 · Cited by 280 · see citing works
The epigenetic landscape related to reactive oxygen species formation in the cardiovascular system
Kietzmann, T., Petry, A., Shvetsova, A., Gerhold, J. M., & Görlach, A. (2017) · British Journal of Pharmacology · doi:10.1111/bph.13792 · Cited by 253 · see citing works
NAD+ homeostasis in human health and disease
Perez, R. Z., Wanders, R. J. A., van Karnebeek, C., & Houtkooper, R. H. (2021) · EMBO Molecular Medicine · doi:10.15252/emmm.202113943 · Cited by 238 · see citing works
PARP-1 involvement in neurodegeneration: A focus on Alzheimer’s and Parkinson’s diseases
Martire, S., Mosca, L., & D’Erme, M. (2015) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2015.04.001 · Cited by 228 · see citing works
Nuclear ADP-Ribosylation and Its Role in Chromatin Plasticity, Cell Differentiation, and Epigenetics
Hottiger, M. O. (2015) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060614-034506 · Cited by 224 · see citing works
Modulating NAD+ metabolism, from bench to bedside
Katsyuba, E., & Auwerx, J. H. (2017) · The EMBO Journal · doi:10.15252/embj.201797135 · Cited by 224 · see citing works
Nicotinamide Riboside—The Current State of Research and Therapeutic Uses
Mehmel, M., Jovanović, N. D., & Spitz, U. P. (2020) · Nutrients · doi:10.3390/nu12061616 · Cited by 225 · see citing works
Opportunities for the repurposing of PARP inhibitors for the therapy of non‐oncological diseases
Berger, N. A., Besson, V. C., Boulares, A. H., Bürkle, A., Chiarugi, A., Clark, R. S. B., Curtin, N. J., Cuzzocrea, S., Dawson, T. M., Dawson, V. L., et al. (2017) · British Journal of Pharmacology · doi:10.1111/bph.13748 · Cited by 212 · see citing works
Poly(ADP-ribose): PARadigms and PARadoxes
Bürkle, A., & Virág, L. (2013) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2012.12.010 · Cited by 197 · see citing works
SIRT1 and SIRT2 Activity Control in Neurodegenerative Diseases
Manjula, R., Anuja, K., & Alcain, F. J. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.585821 · Cited by 193 · see citing works
PARPs in lipid metabolism and related diseases
Szántó, M., Gupte, R., Kraus, W. L., Pacher, P., & Bai, P. (2021) · Progress in Lipid Research · doi:10.1016/j.plipres.2021.101117 · Cited by 184 · see citing works
Self-citationFocus on UV-Induced DNA Damage and Repair—Disease Relevance and Protective Strategies
Kciuk, M., Marciniak, B., Mojzych, M., & Kontek, R. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21197264 · Cited by 168 · see citing works
“Poly-ADP-ribose (PAR) chains are rapidly disassembled by poly (ADP-ribose) glycohydrolase (PARG), allowing the whole event to repeat [55,66].”
BackgroundSirtuins and their Biological Relevance in Aging and Age-Related Diseases
Zhao, L., Cao, J., Hu, K., He, X., Dou, Y., Tong, T., & Han, L. (2020) · Aging and Disease · doi:10.14336/ad.2019.0820 · Cited by 174 · see citing works
Post-translational modifications in mitochondria: protein signaling in the powerhouse
Stram, A. R., & Payne, R. M. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2280-4 · Cited by 149 · see citing works
ARTD1 (PARP1) activation and NAD+ in DNA repair and cell death
Fouquerel, E., & Sobol, R. W. (2014) · DNA repair · doi:10.1016/j.dnarep.2014.09.004 · Cited by 137 · see citing works
Inhibition of poly(ADP-ribosyl)ation in cancer: Old and new paradigms revisited
Lupo, B., & Trusolino, L. (2014) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2014.07.004 · Cited by 131 · see citing works
Sirtuins in neurodegenerative diseases: an update on potential mechanisms
Min, S., Sohn, P., Cho, S.-H., Swanson, R. A., & Gan, L. (2013) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2013.00053 · Cited by 123 · see citing works
Impact of the IVF laboratory environment on human preimplantation embryo phenotype
Gardner, D. K., & Kelley, R. L. (2017) · Journal of Developmental Origins of Health and Disease · doi:10.1017/s2040174417000368 · Cited by 122 · see citing works
The Role of PARPs in Inflammation—And Metabolic—Related Diseases: Molecular Mechanisms and Beyond
Ke, Y., Wang, C., Zhang, J., Zhong, X., Wang, R., Zeng, X., & Ba, X. (2019) · Cells · doi:10.3390/cells8091047 · Cited by 120 · see citing works
Poly(ADP-ribose) polymerases as modulators of mitochondrial activity
Bai, P., Nagy, L., Fodor, T., Liaudet, L., & Pacher, P. (2014) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2014.11.003 · Cited by 119 · see citing works
Self-citationMitochondria in Diabetic Kidney Disease
Ahmad, A. A., Draves, S. O., & Rosca, M. G. (2021) · Cells · doi:10.3390/cells10112945 · Cited by 117 · see citing works
PARP1 orchestrates epigenetic events setting up chromatin domains
Ciccarone, F., Zampieri, M., & Caiafa, P. (2016) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2016.11.010 · Cited by 110 · see citing works
Diabetic Retinopathy: The Role of Mitochondria in the Neural Retina and Microvascular Disease
Miller, D. J., Cascio, M. A., & Rosca, M. G. (2020) · Antioxidants · doi:10.3390/antiox9100905 · Cited by 110 · see citing works
Regulation of Glucose Metabolism by NAD+ and ADP-Ribosylation
Hopp, A.-K., Grüter, P., & Hottiger, M. O. (2019) · Cells · doi:10.3390/cells8080890 · Cited by 107 · see citing works
The taming of PARP1 and its impact on NAD+ metabolism
Hurtado-Bagès, S., Knobloch, G., Ladurner, A. G., & Buschbeck, M. (2020) · Molecular Metabolism · doi:10.1016/j.molmet.2020.01.014 · Cited by 106 · see citing works
Stress-induced chromatin changes in plants: of memories, metabolites and crop improvement
Vriet, C., Hennig, L., & Laloi, C. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1792-z · Cited by 101 · see citing works
Xu, S., Bai, P., Little, P. J., & Liu, P. (2013) · Medicinal Research Reviews · doi:10.1002/med.21300 · Cited by 97 · see citing works
Self-citationHarlan, B. A., Pehar, M., Sharma, D. R., Beeson, G., Beeson, C. C., & Vargas, M. R. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.698779 · Cited by 94 · see citing works
Interplay between Cellular Metabolism and the DNA Damage Response in Cancer
Moretton, A., & Loizou, J. I. (2020) · Cancers · doi:10.3390/cancers12082051 · Cited by 93 · see citing works
SIRT1/PARP1 crosstalk: connecting DNA damage and metabolism
Luna, A., Aladjem, M. I., & Kohn, K. W. (2013) · Genome Integrity · doi:10.1186/2041-9414-4-6 · Cited by 94 · see citing works
Role of endothelial NAD+deficiency in age-related vascular dysfunction
Csiszár, A., Tarantini, S., Yabluchanskiy, A., Balasubramanian, P., Kiss, T., Farkas, E., Baur, J. A., & Ungvari, Z. I. (2019) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00039.2019 · Cited by 93 · see citing works
Szántó, M., & Bai, P. (2020) · Genes & Development · doi:10.1101/gad.334284.119 · Cited by 88 · see citing works
Self-citationExtracellular NAD+ enhances PARP-dependent DNA repair capacity independently of CD73 activity
Wilk, A. M., Hayat, F., Cunningham, R., Li, J., Garavaglia, S., Zamani, L., Ferraris, D. M., Sýkora, P., Andrews, J., Clark, J., et al. (2020) · Scientific Reports · doi:10.1038/s41598-020-57506-9 · Cited by 88 · see citing works
Narne, P., Pandey, V., Simhadri, P. K., & Phanithi, P. B. (2016) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2016.11.007 · Cited by 80 · see citing works
Toward understanding genomic instability, mitochondrial dysfunction and aging
Fakouri, N. B., Hou, Y., Demarest, T. G., Christiansen, L. S., Okur, M. N., Mohanty, J. G., Croteau, D. L., & Bohr, V. A. (2019) · The FEBS Journal · doi:10.1111/febs.14663 · Cited by 77 · see citing works
才原一浩, Kamikubo, R., Ikemoto, K., Uchida, K., & Akagawa, M. (2017) · Biochemistry · doi:10.1021/acs.biochem.7b01185 · Cited by 78 · see citing works
Li, S., Deng, J., Sun, D., Chen, S., Yao, X., Wang, N., Zhang, J., Gu, Q., Zhang, S., Wang, J., et al. (2022) · Redox Biology · doi:10.1016/j.redox.2022.102530 · Cited by 78 · see citing works
Autophagy promotes cell survival by maintaining NAD levels
Kataura, T., Sedlackova, L., Otten, E. G., Kumari, R., Shapira, D., Scialò, F., Stefanatos, R. K. A., Ishikawa, K., Kelly, G., Seranova, E., et al. (2022) · Developmental Cell · doi:10.1016/j.devcel.2022.10.008 · Cited by 78 · see citing works
SIRT3 Regulation Under Cellular Stress: Making Sense of the Ups and Downs
Marcus, J. M., & Andrabi, S. A. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00799 · Cited by 77 · see citing works
Nicotinamide Adenine Dinucleotide Metabolism and Neurodegeneration
Pehar, M., Harlan, B. A., Killoy, K. M., & Vargas, M. R. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7145 · Cited by 77 · see citing works
Compromised DNA repair is responsible for diabetes‐associated fibrosis
Kumar, V., Agrawal, R., Pandey, A., Kopf, S., Höffgen, M., Kaymak, S., Bandapalli, O. R., Gorbunova, V. A., Seluanov, A., Mall, M. A., et al. (2020) · The EMBO Journal · doi:10.15252/embj.2019103477 · Cited by 74 · see citing works
Jiang, J., Liang, S., Zhang, J., Du, Z., Xu, Q., Duan, J., & Sun, Z. (2020) · Journal of Pineal Research · doi:10.1111/jpi.12686 · Cited by 71 · see citing works
Mitochondrial poly(ADP-ribose) polymerase: The Wizard of Oz at work
Brunyánszki, A., Szczęsny, B., Virág, L., & Szabó, C. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.02.024 · Cited by 73 · see citing works
Chandramowlishwaran, P., Vijay, A., Abraham, D., Li, G., Mwangi, S. M., & Srinivasan, S. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.614331 · Cited by 74 · see citing works
Yanagisawa, S., Baker, J. R., Vuppusetty, C., Koga, T., Colley, T., Fenwick, P. S., Donnelly, L., Barnes, P. J., & Ito, K. (2018) · PLoS ONE · doi:10.1371/journal.pone.0193921 · Cited by 70 · see citing works
Metabolic roles of poly(ADP-ribose) polymerases
Vida, A., Márton, J., Mikó, E., & Bai, P. (2016) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2016.12.009 · Cited by 66 · see citing works
Self-citationDecreased Serum Sirtuin-1 in COPD
Yanagisawa, S., Papaioannou, A. Ι., Papaporfyriou, A., Baker, J. R., Vuppusetty, C., Loukides, S., Barnes, P. J., & Ito, K. (2017) · CHEST Journal · doi:10.1016/j.chest.2017.05.004 · Cited by 66 · see citing works
Genomic instability and metabolism in cancer
Li, H., Zimmerman, S. E., & Weyemi, U. (2021) · International review of cytology · doi:10.1016/bs.ircmb.2021.05.004 · Cited by 64 · see citing works
Cellular Compartmentation and the Redox/Nonredox Functions of NAD +
Kulkarni, C. A., & Brookes, P. S. (2019) · Antioxidants and Redox Signaling · doi:10.1089/ars.2018.7722 · Cited by 64 · see citing works
Głombik, K., Stachowicz, A., Ślusarczyk, J., Trojan, E., Budziszewska, B., Suski, M., Kubera, M., Lasoń, W., Wędzony, K., Olszanecki, R., et al. (2015) · Psychoneuroendocrinology · doi:10.1016/j.psyneuen.2015.06.015 · Cited by 64 · see citing works
Hekmatimoghaddam, S., Firoozabadi, A. D., Zare‐Khormizi, M. R., & Pourrajab, F. (2017) · Ageing Research Reviews · doi:10.1016/j.arr.2017.10.001 · Cited by 62 · see citing works
Basse, A. L., Agerholm, M., Farup, J., Dalbram, E., Nielsen, J., Ørtenblad, N., Altıntaş, A., Ehrlich, A. M., Krag, T. O. B., Bruzzone, S., et al. (2021) · Molecular Metabolism · doi:10.1016/j.molmet.2021.101271 · Cited by 62 · see citing works
Diversification of NAD biological role : the importance of location
Stefano, M. D., & Conforti, L. (2013) · FEBS Journal · doi:10.1111/febs.12433 · Cited by 61 · see citing works
Wen, J. J., Yin, Y. W., & Garg, N. J. (2018) · PLoS Pathogens · doi:10.1371/journal.ppat.1007065 · Cited by 61 · see citing works
Ketogenic Diet Modulates NAD+-Dependent Enzymes and Reduces DNA Damage in Hippocampus
Elamin, M., Ruskin, D. N., Masino, S. A., & Sacchetti, P. (2018) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2018.00263 · Cited by 61 · see citing works
The anti-cancer drug doxorubicin induces substantial epigenetic changes in cultured cardiomyocytes
Hanf, A., Oelze, M. W., Manea, A., Li, H., Münzel, T. F., & Daiber, A. (2019) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2019.108834 · Cited by 61 · see citing works
Hegedűs, C., Juhász, T., Fidrus, E., Janka, E. A., Juhász, G., Boros, G., Paragh, G., Uray, K., Emri, G., Remenyik, É., et al. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101808 · Cited by 57 · see citing works
Self-citationKopf, S., Kumar, V., Κender, Ζ., Han, Z., Fleming, T., Herzig, S., & Nawroth, P. P. (2021) · Frontiers in Endocrinology · doi:10.3389/fendo.2021.765201 · Cited by 57 · see citing works
Mejía, S. Á., Baiza-Gutman, L. A., Ortega‐Camarillo, C., Medina-Navarro, R., Sánchez-Becerra, M. C., Santana, L. D., Cruz, M., Pérez, E. H., & Flores, M. D. (2017) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2017.10.048 · Cited by 56 · see citing works
Koentges, C., Cimolai, M. C., Pfeil, K., Wolf, D., Marchini, T., Tarkhnishvili, A., Hoffmann, M. M., Odening, K. E., Diehl, P., Mühlen, C. V. Z., et al. (2019) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2019.06.008 · Cited by 56 · see citing works
Decoding the Rosetta stone of mitonuclear communication
English, J., Son, J. M., Cardamone, M. D., Lee, C., & Perissi, V. (2020) · Pharmacological Research · doi:10.1016/j.phrs.2020.105161 · Cited by 55 · see citing works
Regeneration in the nervous system with erythropoietin
Maiese, K. (2015) · Frontiers in bioscience · doi:10.2741/4408 · Cited by 55 · see citing works
NAD+ Content and Its Role in Mitochondria
Li, W., & Sauve, A. A. (2014) · Methods in molecular biology · doi:10.1007/978-1-4939-1875-1_4 · Cited by 55 · see citing works
Self-citationRole of PARP-1 in mitochondrial homeostasis
Kadam, A. A., Jubin, T., Roychowdhury, R., & Begum, R. (2020) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2020.129669 · Cited by 55 · see citing works
Hegedűs, C., Boros, G., Fidrus, E., Kis, G. N., Antal, M., Juhász, T., Janka, E. A., Jankó, L., Paragh, G., Emri, G., et al. (2019) · Cancers · doi:10.3390/cancers12010005 · Cited by 51 · see citing works
Self-citationLloret, A., & Beal, M. F. (2019) · Neurochemical Research · doi:10.1007/s11064-019-02809-1 · Cited by 52 · see citing works
mTOR may interact with PARP-1 to regulate visible light-induced parthanatos in photoreceptors
Pan, Y.-R., Song, J., Fan, B., Wang, Y., Che, L., Zhang, S., Chang, Y., He, C., & Li, G. (2020) · Cell Communication and Signaling · doi:10.1186/s12964-019-0498-0 · Cited by 52 · see citing works
Yue, R., Chen, G., Xie, G., Hao, L., Guo, W., Sun, X., Jia, W. P., Zhang, Q., Zhou, Z., & Zhong, W. H. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.08.005 · Cited by 50 · see citing works
Qu, H., Lin, K., Wang, H., Wei, H., Ji, B., Yang, Z., Peng, C. X., Xiao, X., & Deng, H. (2016) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201600338 · Cited by 50 · see citing works
The NAD + -Dependent Family of Sirtuins in Cerebral Ischemia and Preconditioning
Khoury, N., Koronowski, K. B., Young, J. I., & Pérez‐Pinzón, M. A. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7258 · Cited by 49 · see citing works
Proteomics approaches to identify mono‐(ADP‐ribosyl)ated and poly(ADP‐ribosyl)ated proteins
Vivelo, C. A., & Leung, A. K. L. (2014) · PROTEOMICS · doi:10.1002/pmic.201400217 · Cited by 49 · see citing works
Deletion of enzymes for de novo NAD + biosynthesis accelerated ovarian aging
Yang, Q., Li, H., Wang, H., Chen, W., Zeng, X., Luo, X., Xu, J., & Sun, Y. (2023) · Aging Cell · doi:10.1111/acel.13904 · Cited by 47 · see citing works
Hu, Y., Wang, H., Wang, Q., & Deng, H. (2013) · Journal of Proteome Research · doi:10.1021/pr4010597 · Cited by 48 · see citing works
A Double-Edged Sword: The Two Faces of PARylation
Kang, M., Park, S., Park, S., Lee, H. G., & Park, J. H. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23179826 · Cited by 46 · see citing works
Mayor, E. (2023) · Frontiers in Aging · doi:10.3389/fragi.2023.1161814 · Cited by 46 · see citing works
Berglund, T., Lindström, A., Aghelpasand, H., Stattin, E., & Ohlsson, A. B. (2015) · Forestry An International Journal of Forest Research · doi:10.1093/forestry/cpv040 · Cited by 46 · see citing works
Espinoza‐Derout, J., Shao, X. M., Bankole, E., Hasan, K. M., Mtume, N., Liu, Y., Sinha‐Hikim, A. P., & Friedman, T. C. (2019) · Frontiers in Endocrinology · doi:10.3389/fendo.2019.00320 · Cited by 47 · see citing works
RecQ helicases and PARP1 team up in maintaining genome integrity
Veith, S., & Mangerich, A. (2014) · Ageing Research Reviews · doi:10.1016/j.arr.2014.12.006 · Cited by 43 · see citing works
Goutham, G., Manikandan, R., Manikandan, B., Raman, T., Chinnasamy, A., Arumugam, M., Setzer, W. N., Daglia, M., Nabavi, S. F., & Nabavi, S. M. (2016) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2016.11.141 · Cited by 45 · see citing works
Sirtuins and their interactions with transcription factors and poly(ADP-ribose) polymerases
Jęśko, H. M., & Strosznajder, R. P. (2016) · Folia Neuropathologica · doi:10.5114/fn.2016.62531 · Cited by 44 · see citing works
Regulatory Effects of NAD + Metabolic Pathways on Sirtuin Activity
Zhang, N., & Sauve, A. A. (2018) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2017.11.012 · Cited by 45 · see citing works
Self-citationRole of Sirtuins in Tumor Angiogenesis
Edatt, L., Poyyakkara, A., Raji, G. R., Ramachandran, V., Shankar, S. S., & Kumar, V. B. S. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2019.01516 · Cited by 43 · see citing works
Chung, J. Y., Kim, O. Y., & Song, J. (2021) · Nutrition Reviews · doi:10.1093/nutrit/nuab118 · Cited by 44 · see citing works
NAD Depletion Mediates Cytotoxicity in Human Neurons With Autophagy Deficiency
Sun, C., Seranova, E., Cohen, M. A., Chipara, M., Roberts, J., Astuti, D., Palhegyi, A. M., Acharjee, A., Sedlackova, L., Kataura, T., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2023.112372 · Cited by 43 · see citing works
Shi, M., Guo, Q., Xiao, Z., Sarengaowa, Xiao, Y., & Feng, K. (2024) · Foods · doi:10.3390/foods13131978 · Cited by 44 · see citing works
Ruiz, P. D., Hamilton, G. A., Park, J. W., & Gamble, M. J. (2019) · Molecular and Cellular Biology · doi:10.1128/mcb.00230-19 · Cited by 40 · see citing works
Chung, H., & Joe, Y. (2014) · Integrative Medicine Research · doi:10.1016/j.imr.2014.09.005 · Cited by 39 · see citing works
Fueling genome maintenance: On the versatile roles of NAD+ in preserving DNA integrity
Ruszkiewicz, J. A., Bürkle, A., & Mangerich, A. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102037 · Cited by 39 · see citing works
Metabolic Plasticity and Epithelial-Mesenchymal Transition
Thomson, T. M., Balcells, C. D., & Cascante, M. (2019) · Journal of Clinical Medicine · doi:10.3390/jcm8070967 · Cited by 38 · see citing works
Magnuson, J. T., Giroux, M. S., Cryder, Z., Gan, J. J., & Schlenk, D. (2020) · Aquatic Toxicology · doi:10.1016/j.aquatox.2020.105518 · Cited by 38 · see citing works
- Authors
- Cantó, C., Sauve, A. A., & Bai, P.
- Affiliations
- Nestlé (Switzerland) (CH)
- Weill Cornell Medicine (US)
- Venue
- Molecular Aspects of Medicine
- Publisher
- Elsevier BV
- Published
- 2013-12
- Volume
- 34
- Issue
- 6
- Pages
- 1168-1201
- ISSN
- 0098-2997 (ISSN-L)
- PMC
- PMC3676863
- OpenAlex
- W1963982942
- Cited by
- 246
- References
- 413
- Citations by year
- 2026: 12 · 2025: 9 · 2024: 15 · 2023: 14 · 2022: 21 · 2021: 27 · 2020: 37 · 2019: 18 · 2018: 16 · 2017: 26 · 2016: 14 · 2015: 17 · 2014: 12 · 2013: 8
- FWCI
- 1.61
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Molecular Aspects of Medicine (publishedVersion)
- PubMed (publishedVersion)
- Repository of the Academy's Library (Library of the Hungarian Academy of Sciences) (acceptedVersion)
- PubMed Central (acceptedVersion)
- University of Debrecen Electronic Archive (University of Debrecen) (submittedVersion, cc-by-nc-nd)
- Funders
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK073466, R21DK094001)
- Topics
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Health Sciences › Medicine › Oncology › PARP inhibition in cancer therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
- Keywords
- poly(ADP-ribose) polymerase, sirtuins, NAD+ metabolism, post-translational modification, transcriptional regulation, oxidative stress response, genome stability, aging, metabolic regulation, pharmacological modulation
- MeSH terms
- Poly(ADP-ribose) Polymerase Inhibitors, Animals, Gene Expression Regulation, Humans, NAD, Poly(ADP-ribose) Polymerases, Protein Binding, Protein Processing, Post-Translational, Oxidative Stress, Sirtuins, Protein Interaction Domains and Motifs
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