Toward understanding genomic instability, mitochondrial dysfunction and aging
Open accessAbstract
The biology of aging is an area of intense research, and many questions remain about how and why cell and organismal functions decline over time. In mammalian cells, genomic instability and mitochondrial dysfunction are thought to be among the primary drivers of cellular aging. This review focuses on the interrelationship between genomic instability and mitochondrial dysfunction in mammalian cells and its relevance to age‐related functional decline at the molecular and cellular level. The importance of oxidative stress and key DNA damage response pathways in cellular aging is discussed, with a special focus on poly (ADP‐ribose) polymerase 1, whose persistent activation depletes cellular energy reserves, leading to mitochondrial dysfunction, loss of energy homeostasis, and altered cellular metabolism. Elucidation of the relationship between genomic instability, mitochondrial dysfunction, and the signaling pathways that connect these pathways/processes are keys to the future of research on human aging. An important component of mitochondrial health preservation is mitophagy, and this and other areas that are particularly ripe for future investigation will be discussed.
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Genomic instability, defective autophagy/mitophagy, and cellular senescence are intertwined with mitochondria-related inflammatory responses.
“Genomic instability, defective autophagy/mitophagy, and cellular senescence, three major hallmarks of aging, are intertwined with mitochondria-related inflammatory responses (Figure 1) (66).”
From Connecting aging biology and inflammation in the omics era (2022) · cites this paper as [66]
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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
RetractedLópez-Otín, C., Blasco, M. A., Partridge, L., Serrano, M., & Kroemer, G. (2013) · Cell · doi:10.1016/j.cell.2013.05.039 · Cited by 14,982 · see citing works
Oxidants, oxidative stress and the biology of ageing
Finkel, T., & Holbrook, N. J. (2000) · Nature · doi:10.1038/35041687 · Cited by 9,413 · see citing works
Ayala, A., Muñoz, M., & Argüelles, S. (2014) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2014/360438 · Cited by 6,557 · see citing works
Mitochondrial Dysfunction and Oxidative Stress in Neurodegenerative Diseases
Lin, M. T., & Beal, M. F. (2006) · Nature · doi:10.1038/nature05292 · Cited by 6,455 · see citing works
Instability and decay of the primary structure of DNA
Lindahl, T. (1993) · Nature · doi:10.1038/362709a0 · Cited by 5,679 · see citing works
Increased oxidative stress in obesity and its impact on metabolic syndrome
Furukawa, S., Fujita, T., Shimabukuro, M., Iwaki, M., Yamada, Y., Nakajima, Y., Nakayama, O., Makishima, M., Matsuda, M., & Shimomura, I. (2004) · Journal of Clinical Investigation · doi:10.1172/jci21625 · Cited by 5,508 · see citing works
TSC2 Mediates Cellular Energy Response to Control Cell Growth and Survival
Inoki, K., Zhu, T., & Guan, K.-L. (2003) · Cell · doi:10.1016/s0092-8674(03)00929-2 · Cited by 3,914 · see citing works
Oxidative Stress, Glutamate, and Neurodegenerative Disorders
Coyle, J. T., & Puttfarcken, P. (1993) · Science · doi:10.1126/science.7901908 · Cited by 3,762 · see citing works
Mitochondrial Fission, Fusion, and Stress
Youle, R. J., & van der Bliek, A. M. (2012) · Science · doi:10.1126/science.1219855 · Cited by 3,674 · 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
ATM and ATR Substrate Analysis Reveals Extensive Protein Networks Responsive to DNA Damage
Matsuoka, S., Ballif, B. A., Smogorzewska, A., McDonald, E. R., Hurov, K. E., Luo, J., Bakalarski, C. E., Zhao, Z., Solimini, N., Lerenthal, Y., et al. (2007) · Science · doi:10.1126/science.1140321 · Cited by 3,075 · see citing works
PINK1 Is Selectively Stabilized on Impaired Mitochondria to Activate Parkin
Narendra, D. P., Jin, S. M., Tanaka, A., Suen, D.-F., Gautier, C. A., Shen, J., Cookson, M. R., & Youle, R. J. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000298 · Cited by 2,944 · see citing works
The ubiquitin kinase PINK1 recruits autophagy receptors to induce mitophagy
Lazarou, M., Sliter, D. A., Kane, L. A., Sarraf, S. A., Wang, C., Burman, J. L., Sideris, D. P., Fogel, A. I., & Youle, R. J. (2015) · Nature · doi:10.1038/nature14893 · Cited by 2,774 · 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
Phosphorylation of ULK1 (hATG1) by AMP-Activated Protein Kinase Connects Energy Sensing to Mitophagy
Egan, D. F., Shackelford, D. B., Mihaylova, M. M., Gelino, S., Kohnz, R. A., Mair, W., Vasquez, D. S., Joshi, A., Gwinn, D. M., Taylor, R., et al. (2011) · Science · doi:10.1126/science.1196371 · Cited by 2,600 · see citing works
Hoeijmakers, J. H. J. (2009) · New England Journal of Medicine · doi:10.1056/nejmra0804615 · Cited by 2,239 · see citing works
Self-consumption: the interplay of autophagy and apoptosis
Mariño, G., Niso-Santano, M., Baehrecke, E. H., & Kroemer, G. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3735 · Cited by 2,172 · see citing works
Mammalian Sirtuins: Biological Insights and Disease Relevance
Haigis, M. C., & Sinclair, D. A. (2010) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev.pathol.4.110807.092250 · Cited by 2,085 · 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
Mitophagy and Quality Control Mechanisms in Mitochondrial Maintenance
Pickles, S., Vigié, P., & Youle, R. J. (2018) · Current Biology · doi:10.1016/j.cub.2018.01.004 · Cited by 2,081 · see citing works
Causes and consequences of replication stress
Zeman, M. K., & Cimprich, K. A. (2014) · Nature Cell Biology · doi:10.1038/ncb2897 · Cited by 2,079 · 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
The multifaceted roles of PARP1 in DNA repair and chromatin remodelling
Ray Chaudhuri, A., & Nussenzweig, A. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.53 · Cited by 1,786 · see citing works
Mitochondrial outer-membrane protein FUNDC1 mediates hypoxia-induced mitophagy in mammalian cells
Liu, L., Feng, D., Chen, G., Chen, M., Zheng, Q., Song, P., Ma, Q., Zhu, C., Wang, R., Qi, W., et al. (2012) · Nature Cell Biology · doi:10.1038/ncb2422 · Cited by 1,689 · 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
Playing the End Game: DNA Double-Strand Break Repair Pathway Choice
Chapman, J. R., Taylor, M. R. G., & Boulton, S. J. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.07.029 · Cited by 1,629 · 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
Repair Pathway Choices and Consequences at the Double-Strand Break
Ceccaldi, R., Rondinelli, B., & D’Andrea, A. D. (2016) · Trends in Cell Biology · doi:10.1016/j.tcb.2015.07.009 · Cited by 1,499 · see citing works
Gomes, A. P., Price, N. L., Ling, A. J. Y., Moslehi, J. J., Montgomery, M. K., Rajman, L., White, J. P., Teodoro, J. S., Wrann, C. D., Hubbard, B. P., et al. (2013) · Cell · doi:10.1016/j.cell.2013.11.037 · Cited by 1,482 · see citing works
Ubiquitin is phosphorylated by PINK1 to activate parkin
Koyano, F., Okatsu, K., Kosako, H., Tamura, Y., Go, E., Kimura, M., Kimura, Y., Tsuchiya, H., Yoshihara, H., Hirokawa, T., et al. (2014) · Nature · doi:10.1038/nature13392 · Cited by 1,477 · see citing works
Aging, energy, and oxidative stress in neurodegenerative diseases
Beal, M. F. (1995) · Annals of Neurology · doi:10.1002/ana.410380304 · Cited by 1,434 · see citing works
Mitochondrial abnormalities in Alzheimer's disease
Hirai, K., Aliev, G., Nunomura, A., Fujioka, H., Russell, R. L., Atwood, C. S., Johnson, A. B., Kress, Y., Vinters, H. V., Tabaton, M., et al. (2001) · The Journal of Neuroscience · doi:10.1523/jneurosci.21-09-03017.2001 · Cited by 1,367 · 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
Nix is a selective autophagy receptor for mitochondrial clearance
Novak, I., Kirkin, V., McEwan, D. G., Zhang, J., Wild, P., Rozenknop, A., Rogov, V., Löhr, F., Popovic, D., Occhipinti, A., et al. (2010) · The EMBO Reports · doi:10.1038/embor.2009.256 · Cited by 1,309 · see citing works
Mitochondrial Dynamics and Metabolic Regulation
Wai, T., & Langer, T. (2016) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2015.12.001 · Cited by 1,304 · see citing works
Zhang, H., Ryu, D., Wu, Y., Gariani, K., Wang, X., Luan, P., D’Amico, D., Ropelle, E. R., Lutolf, M. P., Aebersold, R., et al. (2016) · Science · doi:10.1126/science.aaf2693 · Cited by 1,255 · see citing works
Mouchiroud, L., Houtkooper, R. H., Moullan, N., Katsyuba, E., Ryu, D., Cantó, C., Mottis, A., Jo, Y.-S., Viswanathan, M., Schoonjans, K., et al. (2013) · Cell · doi:10.1016/j.cell.2013.06.016 · Cited by 1,210 · see citing works
Oxidative stress and metabolic disorders: Pathogenesis and therapeutic strategies
Rani, V., Deep, G., Singh, R. K., Palle, K., & Yadav, U. C. S. (2016) · Life Sciences · doi:10.1016/j.lfs.2016.02.002 · Cited by 1,151 · see citing works
SIRT1 and other sirtuins in metabolism
Chang, H.-C., & Guarente, L. (2014) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2013.12.001 · Cited by 1,138 · see citing works
Dynamics of DNA damage response proteins at DNA breaks: a focus on protein modifications
Polo, S. E., & Jackson, S. P. (2011) · Genes & Development · doi:10.1101/gad.2021311 · Cited by 1,092 · see citing works
DNA Repair, Genome Stability, and Aging
Lombard, D. B., Chua, K. F., Mostoslavsky, R., Franco, S., Gostissa, M., & Alt, F. W. (2005) · Cell · doi:10.1016/j.cell.2005.01.028 · Cited by 944 · see citing works
Yao, J., Irwin, R. W., Zhao, L., Nilsen, J., Hamilton, R. T., & Brinton, R. D. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0903563106 · Cited by 940 · see citing works
Kondapalli, C., Kazlauskaite, A., Zhang, N., Woodroof, H. I., Campbell, D. G., Gourlay, R., Burchell, L., Walden, H., Macartney, T. J., Deak, M., et al. (2012) · Open Biology · doi:10.1098/rsob.120080 · Cited by 940 · 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
Mitochondria-Anchored Receptor Atg32 Mediates Degradation of Mitochondria via Selective Autophagy
Okamoto, K., Kondo‐Okamoto, N., & Ohsumi, Y. (2009) · Developmental Cell · doi:10.1016/j.devcel.2009.06.013 · Cited by 867 · 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
Oxidative stress and metabolic syndrome
Roberts, C. K., & Sindhu, K. K. (2009) · Life Sciences · doi:10.1016/j.lfs.2009.02.026 · Cited by 865 · 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
G-quadruplex structures: in vivo evidence and function
Lipps, H. J., & Rhodes, D. (2009) · Trends in Cell Biology · doi:10.1016/j.tcb.2009.05.002 · Cited by 829 · see citing works
Pernas, L. F., & Scorrano, L. (2015) · Annual Review of Physiology · doi:10.1146/annurev-physiol-021115-105011 · Cited by 814 · see citing works
Nucleotide Excision Repair in EukaryotesPreprint
Schärer, O. D. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a012609 · Cited by 801 · see citing works
Atg32 Is a Mitochondrial Protein that Confers Selectivity during Mitophagy
Kanki, T., Wang, K., Cao, Y., Baba, M., & Klionsky, D. J. (2009) · Developmental Cell · doi:10.1016/j.devcel.2009.06.014 · Cited by 798 · see citing works
SLP‐2 is required for stress‐induced mitochondrial hyperfusion
Tondera, D., Grandemange, S., Jourdain, A. A., Karbowski, M., Mattenberger, Y., Herzig, S., Cruz, S. D., Clerc, P., Lauria, I., Merkwirth, C., et al. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.89 · Cited by 767 · see citing works
Hanna, R. A., Quinsay, M. N., Orogo, A. M., Giang, K., Rikka, S., & Gustafsson, Å. B. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.322933 · Cited by 762 · see citing works
On PAR with PARP: cellular stress signaling through poly(ADP-ribose) and PARP-1Preprint
Luo, X., & Kraus, W. L. (2012) · Genes & Development · doi:10.1101/gad.183509.111 · Cited by 725 · see citing works
Ubiquitin-Dependent And Independent Signals In Selective Autophagy
Khaminets, A., Behl, C., & Đikić, I. (2015) · Trends in Cell Biology · doi:10.1016/j.tcb.2015.08.010 · Cited by 716 · see citing works
Defective Mitophagy in XPA via PARP-1 Hyperactivation and NAD+/SIRT1 Reduction
Fang, E. F., Scheibye-Knudsen, M., Brace, L. E., Kassahun, H., SenGupta, T., Nilsen, H., Mitchell, J. R., Croteau, D. L., & Bohr, V. A. (2014) · Cell · doi:10.1016/j.cell.2014.03.026 · Cited by 711 · see citing works
Self-citationNicotinamide riboside is uniquely and orally bioavailable in mice and humans
Trammell, S. A. J., Schmidt, M. S., Weidemann, B. J., Redpath, P., Jaksch, F., Dellinger, R. W., Li, Z., Abel, E. D., Migaud, M. E., & Brenner, C. (2016) · Nature Communications · doi:10.1038/ncomms12948 · Cited by 697 · see citing works
Bioenergetic role of mitochondrial fusion and fission
Westermann, B. (2012) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2012.02.033 · Cited by 687 · see citing works
PINK1 is degraded through the N-end rule pathway
Yamano, K., & Youle, R. J. (2013) · Autophagy · doi:10.4161/auto.24633 · Cited by 669 · see citing works
Role of Telomeres and Telomerase in Aging and Cancer
Shay, J. W. (2016) · Cancer Discovery · doi:10.1158/2159-8290.cd-16-0062 · Cited by 668 · see citing works
Rad51-mediated replication fork reversal is a global response to genotoxic treatments in human cells
Zellweger, R., Dalcher, D., Mutreja, K., Berti, M., Schmid, J. A., Herrador, R., Vindigni, A., & Lopes, M. (2015) · The Journal of Cell Biology · doi:10.1083/jcb.201406099 · Cited by 660 · see citing works
Enhancing mitochondrial proteostasis reduces amyloid-β proteotoxicity
Sorrentino, V., Romani, M., Mouchiroud, L., Beck, J. S., Zhang, H., D’Amico, D., Moullan, N., Potenza, F., Schmid, A. W., Rietsch, S., et al. (2017) · Nature · doi:10.1038/nature25143 · Cited by 630 · see citing works
PARP1-dependent Kinetics of Recruitment of MRE11 and NBS1 Proteins to Multiple DNA Damage Sites
Haince, J.-F., McDonald, D., Rodrigue, A., Déry, U., Masson, J., Hendzel, M. J., & Poirier, G. G. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m706734200 · Cited by 609 · see citing works
Fang, E. F., Kassahun, H., Croteau, D. L., Scheibye-Knudsen, M., Marosi, K., Lu, H., Shamanna, R. A., Kalyanasundaram, S., Bollineni, R. C., Wilson, M. A., et al. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.09.004 · Cited by 575 · see citing works
Self-citationAge-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 · see citing works
Consequences of oxidative stress in age-related macular degeneration
Jarrett, S. G., & Boulton, M. E. (2012) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2012.03.009 · Cited by 537 · see citing works
The dynamic regulation of NAD metabolism in mitochondria
Stein, L. R., & Imai, S. (2012) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2012.06.005 · Cited by 529 · see citing works
Topoisomerase I poisoning results in PARP-mediated replication fork reversal
Chaudhuri, A. R., Hashimoto, Y., Herrador, R., Neelsen, K. J., Fachinetti, D., Bermejo, R., Cocito, A., Costanzo, V., & Lopes, M. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2258 · Cited by 499 · see citing works
Replication fork reversal in eukaryotes: from dead end to dynamic response
Neelsen, K. J., & Lopes, M. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3935 · Cited by 494 · 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
Hou, 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
Self-citationZhu, X.-H., Lu, M., Lee, B.-Y., Ugurbil, K., & Chen, W. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1417921112 · Cited by 468 · 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
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
Li, L., Shi, L., Yang, S., Yan, R., Zhang, D., Yang, J., He, L., Li, W., Yi, X., Sun, L., et al. (2016) · Nature Communications · doi:10.1038/ncomms12235 · Cited by 392 · see citing works
Investigating mitochondrial redox state using NADH and NADPH autofluorescence
Blacker, T. S., & Duchen, M. R. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.08.010 · Cited by 389 · see citing works
Nuclear DNA damage signalling to mitochondria in ageing
Fang, E. F., Scheibye-Knudsen, M., Chua, K. F., Mattson, M. P., Croteau, D. L., & Bohr, V. A. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.14 · Cited by 387 · see citing works
Self-citationDungrawala, H., Rose, K. L., Bhat, K. P., Mohni, K. N., Glick, G. G., Couch, F. B., & Cortez, D. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.07.030 · Cited by 376 · see citing works
Loss of NAD Homeostasis Leads to Progressive and Reversible Degeneration of Skeletal Muscle
Frederick, D. W., Loro, E., Liu, L., Davila, A., Chellappa, K., Silverman, I. M., Quinn, W. J., Gosai, S. J., Tichy, E. D., Davis, J. G., et al. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.07.005 · Cited by 367 · see citing works
Mitochondrial dysfunction in ataxia-telangiectasia
Valentin-Vega, Y. A., MacLean, K. H., Tait-Mulder, J., Milasta, S., Steeves, M., Dorsey, F. C., Cleveland, J. L., Green, D. R., & Kastan, M. B. (2012) · Blood · doi:10.1182/blood-2011-08-373639 · Cited by 365 · see citing works
Oxidative stress in Alzheimer's disease brain: New insights from redox proteomics
Butterfield, D. A., Perluigi, M., & Sultana, R. (2006) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2006.06.026 · Cited by 363 · see citing works
A high-fat diet and NAD(+) activate Sirt1 to rescue premature aging in Cockayne syndrome
Scheibye-Knudsen, M., Mitchell, S. J., Fang, E. F., Iyama, T., Ward, T., Wang, J., Dunn, C. A., Singh, N., Veith, S., Hasan-Olive, M. M., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.10.005 · Cited by 352 · see citing works
Self-citationPARP-1 Activation Requires Local Unfolding of an Autoinhibitory Domain
Dawicki-McKenna, J. M., Langelier, M.-F., DeNizio, J. E., Riccio, A. A., Cao, C. D., Karch, K. R., McCauley, M., Steffen, J. D., Black, B. E., & Pascal, J. M. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.10.013 · Cited by 347 · see citing works
Gong, B., Pan, Y., Vempati, P., Zhao, W., Knable, L., Ho, L., Wang, J., Sastre, M., Ono, K., Sauve, A. A., et al. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.12.005 · Cited by 345 · see citing works
NAD+-Dependent Activation of Sirt1 Corrects the Phenotype in a Mouse Model of Mitochondrial Disease
Cerutti, R., Pirinen, E., Lamperti, C., Marchet, S., Sauve, A. A., Li, W., Leoni, V., Schon, E. A., Dantzer, F., Auwerx, J., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.04.001 · Cited by 343 · see citing works
Hutchinson-Gilford Progeria Syndrome: A premature aging disease caused by LMNA gene mutations
Gonzalo, S., Kreienkamp, R., & Askjaer, P. (2017) · Ageing Research Reviews · doi:10.1016/j.arr.2016.06.007 · Cited by 324 · see citing works
SIRT6 stabilizes DNA-dependent protein kinase at chromatin for DNA double-strand break repair
McCord, R. A., Michishita, E., Hong, T., Berber, E., Boxer, L. D., Kusumoto, R., Guan, S., Shi, X., Gozani, O., Burlingame, A. L., et al. (2009) · Aging · doi:10.18632/aging.100011 · Cited by 313 · see citing works
Self-citationWerner syndrome: Clinical features, pathogenesis and potential therapeutic interventions
Oshima, J., Sidorova, J. M., & Monnat, R. J. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.03.002 · Cited by 310 · see citing works
Poly(ADP-ribose) polymerase-dependent energy depletion occurs through inhibition of glycolysis
Andrabi, S. A., Umanah, G. K. E., Chang, C., Stevens, D. A., Karuppagounder, S. S., Gagné, J.-P., Poirier, G. G., Dawson, V. L., & Dawson, T. M. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1405158111 · Cited by 307 · see citing works
Poly(ADP-ribose) polymerase (PARP-1) has a controlling role in homologous recombination
Schultz, N. D. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg703 · Cited by 301 · 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
Functions of PARylation in DNA Damage Repair Pathways
Wei, H., & Yu, X. (2016) · Genomics Proteomics & Bioinformatics · doi:10.1016/j.gpb.2016.05.001 · Cited by 296 · see citing works
Brown, K. D., Maqsood, S., Huang, J.-Y., Pan, Y., Harkcom, W., Li, W., Sauve, A., Verdin, E., & Jaffrey, S. R. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.11.003 · Cited by 277 · see citing works
Lethal Cardiomyopathy in Mice Lacking Transferrin Receptor in the Heart
Xu, W., Barrientos, T., Mao, L., Rockman, H. A., Sauve, A. A., & Andrews, N. C. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.09.023 · Cited by 274 · see citing works
SIRT1 Regulates the Function of the Nijmegen Breakage Syndrome Protein
Yuan, Z., Zhang, X. M., Sengupta, N., Lane, W. S., & Seto, E. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.05.029 · Cited by 271 · see citing works
The zinc-finger domains of PARP1 cooperate to recognize DNA strand breaks
Ali, A. A. E., Timinszky, G., Arribas-Bosacoma, R., Kozłowski, M., Hassa, P. O., Hassler, M., Ladurner, A. G., Pearl, L. H., & Oliver, A. W. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2335 · Cited by 270 · see citing works
Cockayne syndrome: Clinical features, model systems and pathways
Karikkineth, A. C., Scheibye-Knudsen, M., Fivenson, E., Croteau, D. L., & Bohr, V. A. (2017) · Ageing Research Reviews · doi:10.1016/j.arr.2016.08.002 · Cited by 262 · see citing works
Self-citationHaince, J.-F., Kozlov, S., Dawson, V. L., Dawson, T. M., Hendzel, M. J., Lavin, M. F., & Poirier, G. G. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m608406200 · Cited by 261 · see citing works
PARP1 promotes nucleotide excision repair through DDB2 stabilization and recruitment of ALC1
Pines, A., Vrouwe, M. G., Marteijn, J. A. F., Typas, D., Luijsterburg, M. S., Cansoy, M., Hensbergen, P. J., Deelder, A. M., de Groot, A., Matsumoto, S., et al. (2012) · The Journal of Cell Biology · doi:10.1083/jcb.201112132 · Cited by 255 · see citing works
Molecular Pathways: Overcoming Radiation Resistance by Targeting DNA Damage Response Pathways
Morgan, M. A., & Lawrence, T. S. (2015) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-13-3229 · Cited by 252 · see citing works
Crosstalk between poly(ADP-ribose) polymerase and sirtuin enzymes
Cantó, C., Sauve, A. A., & Bai, P. (2013) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2013.01.004 · Cited by 246 · see citing works
Quinsay, M. N., Thomas, R. L., Lee, Y., & Gustafsson, Å. B. (2010) · Autophagy · doi:10.4161/auto.6.7.13005 · Cited by 239 · see citing works
Liu, D., Pitta, M., Jiang, H., Lee, J.-H., Zhang, G., Chen, X., Kawamoto, E. M., & Mattson, M. P. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.11.020 · Cited by 238 · see citing works
Guan, Y., Wang, S.-R., Huang, X.-Z., Xie, Q.-H., Xu, Y.-Y., Shang, D., & Hao, C.-M. (2017) · Journal of the American Society of Nephrology · doi:10.1681/asn.2016040385 · Cited by 238 · see citing works
Do DNA Double-Strand Breaks Drive Aging?
White, R. R., & Vijg, J. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.08.004 · Cited by 232 · see citing works
Enzymes in the NAD+ Salvage Pathway Regulate SIRT1 Activity at Target Gene Promoters
Zhang, T., Berrocal, J. G., Frizzell, K. M., Gamble, M. J., DuMond, M. E., Krishnakumar, R., Yang, T., Sauve, A. A., & Kraus, W. L. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.016469 · Cited by 230 · 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
Ronson, G. E., Piberger, A. L., Higgs, M. R., Olsen, A. L., Stewart, G. D., McHugh, P. J., Petermann, E., & Lakin, N. D. (2018) · Nature Communications · doi:10.1038/s41467-018-03159-2 · Cited by 227 · see citing works
SIRT1 Regulates UV-Induced DNA Repair through Deacetylating XPA
Fan, W., & Luo, J. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.07.006 · Cited by 223 · 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
The current state of eukaryotic DNA base damage and repair
Bauer, N. C., Corbett, A. H., & Doetsch, P. W. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv1136 · Cited by 216 · see citing works
ARTD1/PARP1 Negatively Regulates Glycolysis by Inhibiting Hexokinase 1 Independent of NAD+ Depletion
Fouquerel, E., Goellner, E. M., Yu, Z., Gagné, J.-P., Barbi de Moura, M., Feinstein, T., Wheeler, D., Redpath, P., Li, J., Romero, G., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.08.036 · Cited by 212 · see citing works
Scheibye‐Knudsen, M., Ramamoorthy, M., Sýkora, P., Maynard, S., Lin, P., Minor, R. K., Wilson, D. M., Cooper, M. P., Spencer, R. G. S., de Cabo, R., et al. (2012) · The Journal of Experimental Medicine · doi:10.1084/jem.20111721 · Cited by 203 · see citing works
Self-citationLong, A. N., Owens, K., Schlappal, A. E., Kristián, T., Fishman, P. S., & Schuh, R. A. (2015) · BMC Neurology · doi:10.1186/s12883-015-0272-x · Cited by 198 · see citing works
PARPs and ADP-Ribosylation: 50 Years … and Counting
Kraus, W. L. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.06.006 · Cited by 191 · see citing works
NAD(+)-dependent repair of damaged DNA by human cell extracts.
Satoh, M. S., Poirier, G. G., & Lindahl, T. L. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53346-9 · Cited by 188 · see citing works
Dellinger, R. W., Santos, S. R., Morris, M., Evans, M., Alminana, D., Guarente, L., & Marcotulli, E. (2017) · npj Aging and Mechanisms of Disease · doi:10.1038/s41514-017-0016-9 · Cited by 181 · see citing works
Aguilar‐Quesada, R., Muñoz‐Gámez, J. A., Martín‐Oliva, D., Peralta, A., Valenzuela, M. T., Matínez-Romero, R., Quiles, R., Murcia, J. M., de MURCIA, G., de Almodóvar, J. M. R., et al. (2007) · BMC Molecular Biology · doi:10.1186/1471-2199-8-29 · Cited by 178 · see citing works
Li, K., Casta, A., Wang, R., Lozada, E., Fan, W., Kane, S. E., Ge, Q., Gu, W. J., Orren, D. K., & Luo, J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m709707200 · Cited by 177 · see citing works
Robu, M., Shah, R. G., Petitclerc, N., Brind’Amour, J., Kandan-Kulangara, F., & Shah, G. M. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1209507110 · Cited by 177 · see citing works
Life Span Extension and Neuronal Cell Protection by Drosophila Nicotinamidase
Balan, V., Miller, G. S., Kaplun, L., Balan, K., Chong, Z.-Z., Li, F., Kaplun, A., VanBerkum, M. F. A., Arking, R., Freeman, D. C., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m804681200 · Cited by 174 · see citing works
Hu, Y., Petit, S. A., Ficarro, S. B., Toomire, K. J., Xie, A., Lim, E., Cao, S. A., Park, E., Eck, M. J., Scully, R., et al. (2014) · Cancer Discovery · doi:10.1158/2159-8290.cd-13-0891 · Cited by 171 · see citing works
NAD<sup>+</sup>metabolism and oxidative stress: the golden nucleotide on a crown of thorns
Massudi, H., Grant, R., Guillemin, G. J., & Braidy, N. (2012) · Redox Report · doi:10.1179/1351000212y.0000000001 · Cited by 158 · see citing works
DDB2 promotes chromatin decondensation at UV-induced DNA damage
Luijsterburg, M. S., Lindh, M., Ács, K., Vrouwe, M. G., Pines, A., van Attikum, H., Mullenders, L. H. F., & Dantuma, N. P. (2012) · The Journal of Cell Biology · doi:10.1083/jcb.201106074 · Cited by 155 · see citing works
Protein Dynamics in Complex DNA Lesions
Aleksandrov, R., Dotchev, A., Poser, I., Krastev, D. B., Georgiev, G. S., Panova, G., Babukov, Y., Danovski, G., Dyankova-Danovska, T., Hubatsch, L., et al. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.02.016 · Cited by 155 · see citing works
Regulation of global genome nucleotide excision repair by SIRT1 through xeroderma pigmentosum C
Ming, M., Shea, C. R., Guo, X., Li, X., Soltani, K., Han, W., & He, Y.-Y. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1010377108 · Cited by 145 · see citing works
Paramasivam, M., Membrino, A., Cogoi, S., Fukuda, H., Nakagama, H., & Xodo, L. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp138 · Cited by 144 · see citing works
Increased poly(ADP-ribose) polymerase activity in lymphoblastoid cell lines from centenarians
Muiras, M.-L., Müller, M. C., Schächter, F., & Bürkle, A. (1998) · Journal of Molecular Medicine · doi:10.1007/s001090050226 · Cited by 140 · see citing works
Surjana, D., Halliday, G. M., & Damian, D. L. (2013) · Carcinogenesis · doi:10.1093/carcin/bgt017 · Cited by 138 · see citing works
Han, B. H., Zhou, M.-L., Johnson, A. W., Singh, I., Liao, F., Vellimana, A. K., Nelson, J. W., Milner, E., Cirrito, J. R., Basak, J., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1414930112 · Cited by 131 · see citing works
Neuroprotective efficacy of aminopropyl carbazoles in a mouse model of amyotrophic lateral sclerosis
Tesla, R., Wolf, H. P., Xu, P., Drawbridge, J., Estill, S. J., Huntington, P., McDaniel, L., Knobbe, W., Burket, A., Tran, S., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1213960109 · Cited by 129 · see citing works
Martin, A. S., Abraham, D. M., Hershberger, K. A., Bhatt, D. P., Mao, L., Cui, H., Liu, J., Liu, X., Muehlbauer, M. J., Grimsrud, P. A., et al. (2017) · JCI Insight · doi:10.1172/jci.insight.93885 · Cited by 128 · see citing works
PARP1 Is a TRF2-associated Poly(ADP-Ribose)Polymerase and Protects Eroded Telomeres
Gomez, M., Wu, J., Schreiber, V., Dunlap, J. R., Dantzer, F., Wang, Y., & Liu, Y. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-07-0672 · Cited by 125 · 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
Cellular NAD Replenishment Confers Marked Neuroprotection Against Ischemic Cell Death
Wang, S., Xing, Z., Vosler, P. S., Yin, H., Li, W., Zhang, F., Signore, A. P., Stetler, R. A., Gao, Y., & Chen, J. (2008) · Stroke · doi:10.1161/strokeaha.107.509158 · Cited by 118 · see citing works
PINK1 Kinase Catalytic Activity Is Regulated by Phosphorylation on Serines 228 and 402
Aerts, L., Craessaerts, K., Strooper, B. D., & Morais, V. A. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.620906 · Cited by 117 · see citing works
Sukhanova, M. V., Abrakhi, S., Joshi, V., Pastré, D., Kutuzov, M. M., Anarbaev, R. O., Curmi, P. A., Hamon, L., & Lavrik, O. I. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv1476 · Cited by 116 · see citing works
Ataxia-telangiectasia (A-T): An emerging dimension of premature ageing
Shiloh, Y., & Lederman, H. M. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.05.002 · Cited by 113 · see citing works
WRN regulates pathway choice between classical and alternative non-homologous end joining
Shamanna, R. A., Lu, H., de Freitas, J. K., Tian, J. Y., Croteau, D. L., & Bohr, V. A. (2016) · Nature Communications · doi:10.1038/ncomms13785 · Cited by 112 · see citing works
Self-citationNuclear p53-mediated repression of autophagy involves PINK1 transcriptional down-regulation
Goiran, T., Duplan, E., Rouland, L., Manaa, W. E., Lauritzen, I., Dunys, J., You, H., Checler, F., & da Costa, C. A. (2018) · Cell Death and Differentiation · doi:10.1038/s41418-017-0016-0 · Cited by 110 · see citing works
Rukhsana Sultana, A., & Butterfield, D. A. (2009) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-009-9241-7 · Cited by 108 · see citing works
CDK1 Enhances Mitochondrial Bioenergetics for Radiation-Induced DNA Repair
Qin, L., Fan, M., Candas, D., Jiang, G., Papadopoulos, S., Tian, L., Woloschak, G. E., Grdina, D. J., & Li, J. J. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.11.015 · Cited by 106 · see citing works
Increased oxidative phosphorylation in response to acute and chronic DNA damage
Brace, L. E., Vose, S. C., Stanya, K. J., Gathungu, R. M., Marur, V. R., Longchamp, A., Treviño-Villarreal, H., Mejia, P., Vargas, D., Inouye, K., et al. (2016) · npj Aging and Mechanisms of Disease · doi:10.1038/npjamd.2016.22 · Cited by 105 · see citing works
Berger, F., Lau, C., & Ziegler, M. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0609211104 · Cited by 104 · see citing works
Lu, H., Shamanna, R. A., de Freitas, J. K., Okur, M. N., Khadka, P., Kulikowicz, T., Holland, P. P., Tian, J. Y., Croteau, D. L., Davis, A. J., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-02146-3 · Cited by 104 · 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
Safety assessment of nicotinamide riboside, a form of vitamin B 3
Conze, D. B., Crespo-Barreto, J., & Kruger, C. L. (2016) · Human & Experimental Toxicology · doi:10.1177/0960327115626254 · Cited by 93 · see citing works
Poly(ADP-ribose) Catabolism Triggers AMP-dependent Mitochondrial Energy Failure
Formentini, L., Macchiarulo, A., Cipriani, G., Camaioni, E., Rapizzi, E., Pellicciari, R., Moroni, F., & Chiarugi, A. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.002931 · Cited by 90 · see citing works
Oxidative metabolism deficiencies in brains of patients with Alzheimer's disease
Hoyer, S. (1996) · Acta Neurologica Scandinavica · doi:10.1111/j.1600-0404.1996.tb05868.x · Cited by 88 · see citing works
Cockayne syndrome group A and B proteins converge on transcription-linked resolution of non-B DNA
Scheibye‐Knudsen, M., Tseng, A. H.-H., Jensen, M. B., Scheibye-Alsing, K., Fang, E. F., Iyama, T., Bharti, S. K., Marosi, K., Froetscher, L., Kassahun, H., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1610198113 · Cited by 88 · see citing works
Self-citationPCAF/GCN5-Mediated Acetylation of RPA1 Promotes Nucleotide Excision Repair
Zhao, M., Geng, R., Guo, X. Y., Yuan, R., Zhou, X. A., Zhong, Y., Huo, Y., Zhou, M., Shen, Q., Li, Y., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.08.015 · Cited by 87 · see citing works
Increased PARP-1 Association with DNA in Alkylation Damaged, PARP-Inhibited Mouse Fibroblasts
Kedar, P. S., Stefanick, D. F., Horton, J. K., & Wilson, S. H. (2012) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-11-0477 · Cited by 82 · see citing works
The PARP inhibitor Olaparib disrupts base excision repair of 5-aza-2′-deoxycytidine lesions
Orta, M. L., Höglund, A., Calderón‐Montaño, J. M., Domı́nguez, I., Burgos‐Morón, E., Visnes, T., Pastor, N., Ström, C. E., López‐Lázaro, M., & Helleday, T. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku638 · Cited by 81 · see citing works
Zhu, G., & Lippard, S. J. (2009) · Biochemistry · doi:10.1021/bi900389b · Cited by 80 · see citing works
Hamity, M. V., White, S. R., Walder, R. Y., Schmidt, M. S., Brenner, C., & Hammond, D. L. (2017) · Pain · doi:10.1097/j.pain.0000000000000862 · Cited by 80 · see citing works
PARP-1 Modulation of mTOR Signaling in Response to a DNA Alkylating Agent
Éthier, C., Tardif, M., Arul, L., & Poirier, G. G. (2012) · PLoS ONE · doi:10.1371/journal.pone.0047978 · Cited by 78 · see citing works
Dregalla, R. C., Zhou, J., Idate, R., Battaglia, C. L. R., Liber, H. L., & Bailey, S. M. (2010) · Aging · doi:10.18632/aging.100210 · Cited by 78 · see citing works
Fischer, J. M. F., Popp, O., Gebhard, D., Veith, S., Fischbach, A., Beneke, S., Leitenstorfer, A., Bergemann, J., Scheffner, M., Ferrando‐May, E., et al. (2014) · The FEBS Journal · doi:10.1111/febs.12885 · Cited by 72 · see citing works
Bloom’s syndrome: Why not premature aging?
de Renty, C., & Ellis, N. A. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.05.010 · Cited by 72 · see citing works
Disruption of PARP1 function inhibits base excision repair of a sub-set of DNA lesions
Reynolds, P., Cooper, S., Lomax, M. E., & O’Neill, P. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv250 · Cited by 66 · see citing works
Lü, L., Tang, L., Wei, W., Hong, Y., Chen, H., Ying, W., & Chen, S. (2014) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2014.1842 · Cited by 62 · see citing works
Acetylation of 53BP1 dictates the DNA double strand break repair pathway
Guo, X. Y., Bai, Y., Zhao, M., Zhou, M., Shen, Q., Yun, C., Zhang, H., Zhu, W., & Wang, J. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx1208 · Cited by 61 · see citing works
Weinfeld, M., Chaudhry, M. A., D’Amours, D., Pelletier, J. D., Poirier, G. G., Povirk, L. F., Lees‐Miller, S. P., & Pelletier, J. D. (1997) · Radiation Research · doi:10.2307/3579534 · Cited by 53 · see citing works
Aging in Rothmund-Thomson syndrome and related RECQL4 genetic disorders
Lu, L., Jin, W., & Wang, L. L. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.06.002 · Cited by 52 · see citing works
Robu, M., Shah, R. G., Purohit, N. K., Zhou, P., Naegeli, H., & Shah, G. M. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1706981114 · Cited by 50 · see citing works
Linking DNA Damage, NAD + /SIRT1, and Aging
Guarente, L. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.10.015 · Cited by 45 · see citing works
NAD <sup>+</sup> : The convergence of DNA repair and mitophagy
Fang, E. F., & Bohr, V. A. (2017) · Autophagy · doi:10.1080/15548627.2016.1257467 · Cited by 45 · see citing works
Self-citationGenome instability: a conserved mechanism of ageing?
Vijg, J., Dong, X., Milholland, B., & Zhang, L. (2017) · Essays in Biochemistry · doi:10.1042/ebc20160082 · Cited by 45 · see citing works
Berger, N. A., Berger, S. J., Catino, D. M., et al. (1985) · Journal of Clinical Investigation · doi:10.1172/jci111750 · Cited by 41 · see citing works
Wakade, C. G., Chong, R. K. Y., Bradley, E., & Morgan, J. C. (2015) · Clinical Case Reports · doi:10.1002/ccr3.232 · Cited by 41 · see citing works
Maltseva, E. A., Rechkunova, N. I., Sukhanova, M. V., & Lavrik, O. I. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.646638 · Cited by 38 · see citing works
Alisky, J. M. (2005) · Nutritional Neuroscience · doi:10.1080/10284150500484638 · Cited by 38 · see citing works
Guliaev, A. B. (2002) · Nucleic Acids Research · doi:10.1093/nar/gkf494 · Cited by 35 · see citing works
Phenotypic Characterization of Parp-1 and Parp-2 Deficient Mice and Cells
Boehler, C., Gauthier, L., Yélamos, J., et al. (2011) · Methods in molecular biology · doi:10.1007/978-1-61779-270-0_19 · Cited by 31 · see citing works
Poly(ADP-Ribose) Polymerases in Aging - Friend or Foe?
Vida, A., Abdul-Rahman, O., Mikó, E., Brunyánszki, A., & Bai, P. (2016) · Current Protein and Peptide Science · doi:10.2174/1389203717666160419144959 · Cited by 28 · see citing works
Poly(ADP-ribose) polymerase can bind melphalan damaged DNA.
Bramson, J. L., Prévost, J., Malapetsa, A., Noe, A., Poirier, G. G., Desnoyers, S., Alaoui-Jamali, M., & Panasci, L. (1993) · PubMed · Cited by 24 · see citing works
Batra, V., & Kislay, B. (2013) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2013.07.001 · Cited by 16 · see citing works
The DNA damage-inducible C. elegans tankyrase is a nuclear protein closely linked to chromosomes
White, C. I., Gagnon, S., St-Laurent, J.-F., et al. (2008) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-008-9986-z · Cited by 13 · see citing works
SIRT1 activation mediates heat-induced survival of UVB damaged Keratinocytes
Calapre, L., Gray, E. S., Kurdykowski, S., David, A. S., Descargues, P., & Ziman, M. R. (2017) · BMC Dermatology · doi:10.1186/s12895-017-0060-y · Cited by 7 · see citing works
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Autophagy and the hallmarks of aging
Kaushik, S., Tasset, I., Arias, E., Pampliega, O., Wong, E., Martinez-Vicente, M., & Cuervo, A. M. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101468 · Cited by 285 · see citing works
Connecting aging biology and inflammation in the omics era
Walker, K. A., Basisty, N., Wilson, D. M., & Ferrucci, L. (2022) · Journal of Clinical Investigation · doi:10.1172/jci158448 · Cited by 189 · see citing works
The mitochondrial permeability transition: Nexus of aging, disease and longevity
Rottenberg, H., & Hoek, J. B. (2021) · Cells · doi:10.3390/cells10010079 · Cited by 94 · see citing works
Kumar, P., Osahon, O. W., & Sekhar, R. V. (2022) · Nutrients · doi:10.3390/nu14051114 · Cited by 83 · see citing works
The link between Mitochondria and Sarcopenia
Kamarulzaman, N. T., & Makpol, S. (2025) · Journal of Physiology and Biochemistry · doi:10.1007/s13105-024-01062-7 · Cited by 33 · see citing works
- Authors
- Fakouri, N. B., Hou, Y., Demarest, T. G., Christiansen, L. S., Okur, M. N., Mohanty, J. G., Croteau, D. L., & Bohr, V. A.
- Affiliations
- National Institutes of Health (US)
- Corresponding author
- Bohr, Vilhelm A.
- ORCID
- Venue
- The FEBS Journal
- Publisher
- Wiley
- Published
- 2018-10-08
- Volume
- 286
- Issue
- 6
- Pages
- 1058-1073
- ISSN
- 1742-464X (ISSN-L)
- 1742-4658
- OpenAlex
- W2892134972
- Cited by
- 77
- References
- 181
- Citations by year
- 2026: 5 · 2025: 11 · 2024: 9 · 2023: 10 · 2022: 14 · 2021: 12 · 2020: 9 · 2019: 6 · 2018: 1
- FWCI
- 0.69
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- public-domain
- onlinelibrary.wiley.com/termsAndConditions#vor (vor)
- Locations
- FEBS Journal (publishedVersion, public-domain)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Aging › Genetics, Aging, and Longevity in Model Organisms
- Health Sciences › Medicine › Physiology › Telomeres, Telomerase, and Senescence
- Keywords
- genomic instability, mitochondrial dysfunction, cellular aging, oxidative stress, DNA damage response, PARP1, energy homeostasis, cellular metabolism, mitophagy, age-related functional decline
- MeSH terms
- Aging, Animals, Energy Metabolism, Homeostasis, Humans, Mitochondria, Poly(ADP-ribose) Polymerases, Oxidative Stress, Genomic Instability, Mitophagy
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