The DOI matches its Crossref record; 20 of the 20 references it cites were found in a registry or an index.
The Role of PARP-1 and PARP-2 Enzymes in Metabolic Regulation and Disease
Open accessAbstract
While originally described as DNA damage repair agents, recent data suggest a role for poly(ADP-ribose) polymerase (PARP) enzymes in metabolic regulation by influencing mitochondrial function and oxidative metabolism. Here we review how PARP activity has a major metabolic impact and the role of PARP-1 and PARP-2 in diverse metabolic complications.
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In the citing paper
“Among all the PARPs, only PARP1, PARP2 and PARP3 localize to the nucleus (FIG. 1b) in response to early DNA damage and have a key role in DNA damage repair25–27 (Supplementary Box 2).”
From NAD+ metabolism and its roles in cellular processes during ageing (2021) · cites this paper as [25]
In the citing paper
“PARP2 activity may also influence NAD+ bioavailability25,26.”
From NAD+ metabolism and its roles in cellular processes during ageing (2021) · cites this paper as [25]
In the citing paper
“PARP1 is the main PARP enzyme in mammalian tissues and utilize NAD+ during its catalysis”
From A Potent and Specific CD38 Inhibitor Ameliorates Age-Related Metabolic Dysfunction by Reversing Tissue NAD+ Decline (2018) · cites this paper as Bai and Cantó, 2012
In the citing paper
“several studies have proposed that PARP1 inhibition can be used to promote increases in cellular levels of NAD+ by decreasing its degradation”
From A Potent and Specific CD38 Inhibitor Ameliorates Age-Related Metabolic Dysfunction by Reversing Tissue NAD+ Decline (2018) · cites this paper as Bai and Cantó, 2012
In the citing paper
“One strategy to increase NAD+ levels consists of the inhibition of alternative NAD+ consuming enzymes, such as poly(ADP-ribose) polymerase-1 (PARP-1) (Bai and Canto, 2012), which is involved in DNA damage detection and repair.”
From Pharmacological Inhibition of poly(ADP-ribose) polymerases improves fitness and mitochondrial function in skeletal muscle (2014) · cites this paper as Bai and Canto, 2012
Citations
Cites
1 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
RetractedCircadian Control of the NAD + 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
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
Self-citationThe PARP Side of the Nucleus: Molecular Actions, Physiological Outcomes, and Clinical Targets
Krishnakumar, R., & Kraus, W. L. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.06.017 · Cited by 877
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
Self-citationBurkart, 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
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
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 313
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 260
Self-citationYonemura, Y., Takashima, T., Miwa, K., Miyazaki, I., Yamamoto, H., & Okamoto, H. (1984) · Diabetes · doi:10.2337/diab.33.4.401 · Cited by 170
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Zhang, J., Tufail, M., Deng, Y., Ling, H.-J., Peng, L., Wu, J., Zeng, D., Zhang, Y., He, L., Peng, H., et al. (2026) · Drug Resistance Updates · doi:10.1016/j.drup.2026.101432
Computational design, synthesis, and in vitro evaluation of thiadiazole-derived PARP-1 inhibitors
Balachandran, H., Arun, S., Lakshmanan, K., Purohit, D., Byran, G., & Rajagopal, K. (2026) · Journal of Receptors and Signal Transduction · doi:10.1080/10799893.2026.2697740
Metabolites with a message: impacts on epigenetics and implications for epimetabopathies
Banerjee, I., Mondal, A., Kamat, S. S., & Das, C. (2026) · EMBO Reports · doi:10.1038/s44319-026-00891-5
Tankyrase‐2 regulates adipocyte differentiation through AMPK / mTOR signaling
Rauch, B., Ujlaki, G., Póliska, S., Murahwa, N., Kovács, P., Pettkó‐Szandtner, A., Uray, K., & Bai, P. (2026) · FEBS Journal · doi:10.1111/febs.70676
Self-citationLi, G., Antunes, I. F., Ming, Z., Wu, C., Cornelissen, B., & de Vries, E. F. J. (2026) · Neurotherapeutics · doi:10.1016/j.neurot.2026.e01044
Timbury, W., Gettings, S. M., Shek, R., Lindsay, C. D., Sharma, R., Najim, M., & Bourbia, N. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.08.11.735255
May, M., Fabela, R. F., & Tomanek, L. (2026) · Frontiers in Ecology and Evolution · doi:10.3389/fevo.2026.1914093
METTL3-mediated m6A modification of PARP2 accelerates hepatocellular carcinoma progression
Li, M., Zhao, Y., & Li, Y. (2026) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2026.118069
Gong, F., Yu, M., Chen, Z., Li, M., Sang, X., & Yan, Y. (2026) · The Kaohsiung Journal of Medical Sciences · doi:10.1002/kjm2.70275
Ducray, A. D., Chaabene, R. B., Jamaati, A., Capstick, M., & Mevissen, M. (2026) · NeuroToxicology · doi:10.1016/j.neuro.2026.103591
BindingDB (2024) · UC San Diego · doi:10.7270/q23f4v4p
BindingDB (2023) · UC San Diego · doi:10.7270/q2k93cjv
Metadata
- Authors
- Bai, P., & Cantó, C.
- Affiliations
- University of Debrecen (HU)
- Nestlé (Switzerland) (CH)
- Corresponding author
- Bai, Péter
- Cantó, Carles
- Venue
- Cell Metabolism
- Publisher
- Elsevier BV
- Published
- 2012-09
- Volume
- 16
- Issue
- 3
- Pages
- 290-295
- ISSN
- 1550-4131 (ISSN-L)
- OpenAlex
- W2086531857
- Cited by
- 312
- References
- 20
- Citations by year
- 2026: 20 · 2025: 19 · 2024: 27 · 2023: 26 · 2022: 24 · 2021: 26 · 2020: 18 · 2019: 25 · 2018: 20 · 2017: 17 · 2016: 22 · 2015: 21 · 2014: 28 · 2013: 18 · 2012: 1
- FWCI
- 10.75
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell Metabolism (publishedVersion)
- PubMed (publishedVersion)
- University of Debrecen Electronic Archive (University of Debrecen) (submittedVersion)
- Topics
- Health Sciences › Medicine › Oncology › PARP inhibition in cancer therapy
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Keywords
- PARP1, PARP2, poly(ADP-ribose) polymerase, metabolic regulation, mitochondrial function, oxidative metabolism, DNA repair, metabolic disorders
- MeSH terms
- Poly (ADP-Ribose) Polymerase-1, Energy Metabolism, Humans, Metabolic Diseases, Mitochondria, Poly(ADP-ribose) Polymerases, Transcription Factors, Metabolic Networks and Pathways, Sirtuin 1
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