The DOI matches its Crossref record; 406 of the 413 references it cites were found in a registry or an index.
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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“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]
In the citing paper
“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]
In the citing paper
“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]
In the citing paper
“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]
In the citing paper
“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]
In the citing paper
“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]
In the citing paper
“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]
In the citing paper
“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]
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Citations
Cites
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
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
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Nitric oxide synthases: regulation and function
Forstermann, U., & Sessa, W. C. (2012) · European Heart Journal · doi:10.1093/eurheartj/ehr304 · Cited by 4,409
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
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Nathan, C. (1992) · The FASEB Journal · doi:10.1096/fasebj.6.12.1381691 · Cited by 4,350
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
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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
Research works printed but not linked: 1
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Cited by
Sorted by citations
Cantó, C., Menzies, K. J., & Auwerx, J. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.05.023 · Cited by 1,648
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
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 928
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 509
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
Metadata
- 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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