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The PARP superfamily
Open accessAbstract
Poly(ADP‐ribosyl)ation is an immediate DNA‐damage‐dependent post‐translational modification of histones and other nuclear proteins that contributes to the survival of injured proliferating cells. Poly(ADP‐ribose) polymerases (PARPs) now constitute a large family of 18 proteins, encoded by different genes and displaying a conserved catalytic domain in which PARP‐1 (113 kDa), the founding member, and PARP‐2 (62 kDa) are so far the sole enzymes whose catalytic activity has been shown to be immediately stimulated by DNA strand breaks. A large repertoire of sequences encoding novel PARPs now extends considerably the field of poly(ADP‐ribosyl)ation reactions to various aspects of the cell biology including cell proliferation and cell death. Some of these new members interact with each other, share common partners and common subcellular localizations suggesting possible fine tuning in the regulation of this post‐translational modification of proteins. This review summarizes our present knowledge of this emerging superfamily, which might ultimately improve pharmacological strategies to enhance both antitumor efficacy and the treatment of a number of inflammatory and neurodegenerative disorders. A provisional nomenclature is proposed. BioEssays 26:882–893, 2004. © 2004 Wiley Periodicals, Inc.
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Cites
DNA double-stranded breaks induce histone H2AX phosphorylation on serine 139
Rogakou, E. P., Pilch, D. R., Orr, A. H., Ivanova, V. S., & Bonner, W. M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.10.5858 · Cited by 5,438
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
Calabrese, C. R., Almassy, R., Barton, S., Batey, M. A., Calvert, A. H., Canan-Koch, S., Durkacz, B. W., Hostomsky, Z., Kumpf, R. A., Kyle, S., et al. (2004) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/djh005 · Cited by 487
A Role of Poly (ADP-Ribose) Polymerase in NF- B Transcriptional Activation
Hassa, P. O., & Hottiger, M. O. (1999) · Biological Chemistry · doi:10.1515/bc.1999.118 · Cited by 296
HIF-1: A Target For Cancer, Ischemia and Inflammation—Too Good to be True?
Melillo, G. (2004) · Cell Cycle · doi:10.4161/cc.3.2.689 · Cited by 247
Crystal structure of the catalytic fragment of murine poly(ADP-ribose) polymerase-2
Oliver, A. W. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh215 · Cited by 127
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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
Galluzzi, L., Vitale, I., Abrams, J. M., Alnemri, E. S., Baehrecke, E. H., Blagosklonny, M. V., Dawson, T. M., Dawson, V. L., El-Deiry, W. S., Fulda, S., et al. (2012) · Cell Death & Differentiation · doi:10.1038/cdd.2011.96 · Cited by 2,421
Audeh, M. W., Carmichael, J., Penson, R. T., Friedlander, M., Powell, B., Bell-McGuinn, K. M., Scott, C., Weitzel, J. N., Oaknin, A., Loman, N., et al. (2010) · The Lancet · doi:10.1016/s0140-6736(10)60893-8 · Cited by 2,279
Poly(ADP-ribose): novel functions for an old molecule
Schreiber, V., Dantzer, F., Ame, J.-C., & de Murcia, G. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1963 · Cited by 1,915
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Abrahams, B. S., & Geschwind, D. H. (2008) · Nature Reviews Genetics · doi:10.1038/nrg2346 · Cited by 1,866
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
PARP inhibition: PARP1 and beyond
Rouleau, M., Patel, A., Hendzel, M. J., Kaufmann, S. H., & Poirier, G. G. (2010) · Nature Reviews Cancer · doi:10.1038/nrc2812 · Cited by 1,298
PARP-1 cleavage fragments: signatures of cell-death proteases in neurodegeneration
Chaitanya, G. V., Alexander, J. S., & Babu, P. P. (2010) · Cell Communication and Signaling · doi:10.1186/1478-811x-8-31 · Cited by 926
Awakening guardian angels: drugging the p53 pathway
Brown, C. J., Lain, S., Verma, C. S., Fersht, A. R., & Lane, D. P. (2009) · Nature Reviews Cancer · doi:10.1038/nrc2763 · Cited by 881
Bacterial resistance to antibiotics: Enzymatic degradation and modification
WRIGHT, G. (2005) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2005.04.002 · Cited by 897
The 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 836
Poly(ADP-ribosyl)ation by PARP-1: `PAR-laying' NAD+ into a nuclear signal
Kim, M. Y., Zhang, T., & Kraus, W. L. (2005) · Genes & Development · doi:10.1101/gad.1331805 · Cited by 802
PARPs and ADP-ribosylation: recent advances linking molecular functions to biological outcomes
Gupte, R., Liu, Z., & Kraus, W. L. (2017) · Genes & Development · doi:10.1101/gad.291518.116 · Cited by 681
“Furthermore, they suggest that PARP-14 and PARP-15 may have gone through multiple cycles of gene birth and loss, supporting the theory that they are evolving rapidly in response to viral conflicts (Daugherty et al. 2014).”
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Morales, J., Li, L., Fattah, F. J., Dong, Y., Bey, E. A., Patel, M., Gao, J., & Boothman, D. A. (2014) · Critical Reviews in Eukaryotic Gene Expression · doi:10.1615/critreveukaryotgeneexpr.2013006875 · Cited by 608
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Santivasi, W. L., & Xia, F. (2014) · Antioxidants & Redox Signaling · doi:10.1089/ars.2013.5668 · Cited by 593
Menear, K. A., Adcock, C., Boulter, R., Cockcroft, X.-L., Copsey, L., Cranston, A., Dillon, K. J., Drzewiecki, J., Garman, S., Gomez, S., et al. (2008) · Journal of Medicinal Chemistry · doi:10.1021/jm8001263 · Cited by 584
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Parthanatos, a messenger of death
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Gottschalk, A. J., Timinszky, G., Kong, S. E., Jin, J., Cai, Y., Swanson, S. K., Washburn, M. P., Florens, L., Ladurner, A. G., Conaway, J. W., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0906920106 · Cited by 356
Substrate-Assisted Catalysis by PARP10 Limits Its Activity to Mono-ADP-Ribosylation
Kleine, H., Poreba, E., Lesniewicz, 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 338
Predictive biomarkers: a paradigm shift towards personalized cancer medicine
La Thangue, N. B., & Kerr, D. J. (2011) · Nature Reviews Clinical Oncology · doi:10.1038/nrclinonc.2011.121 · Cited by 332
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., Reina-San-Martin, B., & Caldecott, K. W. (2011) · Molecular Cell · doi:10.1016/j.molcel.2010.12.006 · Cited by 326
Kummar, S., Kinders, R., Gutierrez, M. E., Rubinstein, L., Parchment, R. E., Phillips, L. R., Ji, J., Monks, A., Low, J. A., Chen, A., et al. (2009) · Journal of Clinical Oncology · doi:10.1200/jco.2008.19.7681 · Cited by 326
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Wang, Y., Jiang, X., Feng, F., Liu, W., & Sun, H. (2020) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2019.08.001 · Cited by 335
Jones, P., Altamura, S., Boueres, J., Ferrigno, F., Fonsi, M., Giomini, C., Lamartina, S., Monteagudo, E., Ontoria, J. M., Orsale, M. V., et al. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm901188v · Cited by 316
Zarghooni, M., Bartels, U., Lee, E., Buczkowicz, P., Morrison, A., Huang, A., Bouffet, E., & Hawkins, C. (2010) · Journal of Clinical Oncology · doi:10.1200/jco.2009.25.5463 · Cited by 313
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Lord, C. J., & Ashworth, A. (2008) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2008.06.016 · Cited by 289
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Virág, L., Robaszkiewicz, A., Rodriguez-Vargas, J. M., & Oliver, F. J. (2013) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2013.01.007 · Cited by 273
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Hochegger, H., Dejsuphong, D., Fukushima, T., Morrison, C., Sonoda, E., Schreiber, V., Zhao, G. Y., Saberi, A., Masutani, M., Adachi, N., et al. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601015 · Cited by 276
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HPF1 completes the PARP active site for DNA damage-induced ADP-ribosylation
Suskiewicz, M. J., Zobel, F., Ogden, T. E. H., Fontana, P., Ariza, A., Yang, J.-C., Zhu, K., Bracken, L., Hawthorne, W. J., Ahel, D., et al. (2020) · Nature · doi:10.1038/s41586-020-2013-6 · Cited by 264
Kummar, S., Chen, A., Ji, J., Zhang, Y., Reid, J. M., Ames, M., Jia, L., Weil, M., Speranza, G., Murgo, A. J., et al. (2011) · Cancer Research · doi:10.1158/0008-5472.can-11-1227 · Cited by 259
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Otto, H., Reche, P. A., Bazan, F., Dittmar, K., Haag, F., & Koch-Nolte, F. (2005) · BMC Genomics · doi:10.1186/1471-2164-6-139 · Cited by 259
Tankyrase-1 polymerization of poly(ADP-ribose) is required for spindle structure and function
Chang, P., Coughlin, M., & Mitchison, T. J. (2005) · Nature Cell Biology · doi:10.1038/ncb1322 · Cited by 259
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
PARP-1, PARP-2 and ATM in the DNA damage response: functional synergy in mouse development
Huber, A., Bai, P., Murcia, J. M. D., & Murcia, G. D. (2004) · DNA Repair · doi:10.1016/j.dnarep.2004.06.002 · Cited by 222
Self-citationPARP inhibitors: review of mechanisms of action and BRCA1/2 mutation targeting
Dziadkowiec, K. N., Gąsiorowska, E., Nowak-Markwitz, E., & Jankowska, A. (2016) · Menopausal Review · doi:10.5114/pm.2016.65667 · Cited by 191
Cisplatin Resistance Associated with PARP Hyperactivation
Michels, J., Vitale, I., Galluzzi, L., Adam, J., Olaussen, K. A., Kepp, O., Senovilla, L., Talhaoui, I., Guegan, J., Enot, D. P., et al. (2013) · Cancer Research · doi:10.1158/0008-5472.can-12-3000 · Cited by 176
Mashimo, M., Kato, J., & Moss, J. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1312783110 · Cited by 162
PARP-1 activation in the ERK signaling pathway
COHENARMON, M. (2007) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2007.08.005 · Cited by 137
Pathophysiological role of different tubular epithelial cell death modes in acute kidney injury
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Bochum, S., Berger, S., & Martens, U. M. (2018) · Recent Results in Cancer Research · doi:10.1007/978-3-319-91442-8_15 · Cited by 104
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Ye, Y., Xiao, L., Wang, S.-J., Yue, W., Yin, Q.-S., Sun, M.-Y., Xia, W., Shao, Z.-Y., & Zhang, H. (2016) · Oncotarget · doi:10.18632/oncotarget.6473 · Cited by 47
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Metadata
- Authors
- Amé, J., Spenlehauer, C., & de Murcia, G.
- Venue
- BioEssays
- Publisher
- Wiley
- Published
- 2004-07-19
- Volume
- 26
- Issue
- 8
- Pages
- 882-893
- ISSN
- 0265-9247 (ISSN-L)
- 1521-1878
- OpenAlex
- W2057706543
- Cited by
- 1,459
- References
- 6
- FWCI
- 4.05
- Type
- journal article
- Language
- en
- Open access
- bronze
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