The DOI matches its Crossref record; 317 of the 318 references it cites were found in a registry or an index.
Coordination of DNA single strand break repair
Open accessAbstract
The genetic material of all organisms is susceptible to modification. In some instances, these changes are programmed, such as the formation of DNA double strand breaks during meiotic recombination to generate gamete variety or class switch recombination to create antibody diversity. However, in most cases, genomic damage is potentially harmful to the health of the organism, contributing to disease and aging by promoting deleterious cellular outcomes. A proportion of DNA modifications are caused by exogenous agents, both physical (namely ultraviolet sunlight and ionizing radiation) and chemical (such as benzopyrene, alkylating agents, platinum compounds and psoralens), which can produce numerous forms of DNA damage, including a range of "simple" and helix-distorting base lesions, abasic sites, crosslinks and various types of phosphodiester strand breaks. More significant in terms of frequency are endogenous mechanisms of modification, which include hydrolytic disintegration of DNA chemical bonds, attack by reactive oxygen species and other byproducts of normal cellular metabolism, or incomplete or necessary enzymatic reactions (such as topoisomerases or repair nucleases). Both exogenous and endogenous mechanisms are associated with a high risk of single strand breakage, either produced directly or generated as intermediates of DNA repair. This review will focus upon the creation, consequences and resolution of single strand breaks, with a particular focus on two major coordinating repair proteins: poly(ADP-ribose) polymerase 1 (PARP1) and X-ray repair cross-complementing protein 1 (XRCC1).
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“DNA of mammal cells experiences over 105 modifications per day, many of which are ROS-related single-strand breaks that are detected by the DNA-break sensor poly(ADP-ribose) polymerase 1 (PARP1), and ultimately resolved by defined repair mechanisms (68).”
From Connecting aging biology and inflammation in the omics era (2022) · cites this paper as [68]
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
1 retracted
Items 201–317 of 317
Cloning and expression of cDNA for human poly(ADP-ribose) polymerase.
Alkhatib, H., Chen, D. F., Cherney, B., Bhatia, K. G., Notario, V., Giri, C., Stein, G. S., Slattery, E., Roeder, R. G., & Smulson, M. E. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.5.1224 · Cited by 101
AP-site cleavage activity of tyrosyl-DNA phosphodiesterase 1
Lebedeva, N. A., Rechkunova, N. I., & Lavrik, O. I. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.01.032 · Cited by 100
Parsons, J. L., Dianova, I. I., Allinson, S. L., & Dianov, G. L. (2005) · FEBS Journal · doi:10.1111/j.1742-4658.2005.04628.x · Cited by 99
Interaction of the Transcription Factor YY1 with Human Poly(ADP-Ribosyl) Transferase
Oei, S. L., Griesenbeck, J., Schweiger, M., Babich, V., Kropotov, A., & Tomilin, N. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.7621 · Cited by 99
Lan, L., Nakajima, S., Wei, L., Sun, L., Hsieh, C.-L., Sobol, R. W., Bruchez, M. P., Houten, B. V., Yasui, A., & Levine, A. S. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt1233 · Cited by 98
Refined mapping of the three DNA repair genes, ERCC1, ERCC2, and XRCC1, on human chromosome 19
Mohrenweiser, H. W., Carrano, A. V., Fertitta, A., Perry, B., Thompson, L. H., Tucker, J. D., & Weber, C. A. (2008) · Cytogenetics and Cell Genetics · doi:10.1159/000132829 · Cited by 98
Mitochondrial DNA ligase III function is independent of Xrcc1
Lakshmipathy, U. (2000) · Nucleic Acids Research · doi:10.1093/nar/28.20.3880 · Cited by 95
Zdzienicka, M. Z., van der Schans, G. P., Natarajan, A. T., Thompson, L. H., Neuteboom, I., & Simons, J. W. I. M. (1992) · Mutagenesis · doi:10.1093/mutage/7.4.265 · Cited by 95
Harris, J. L., Jakob, B., Taucher-Scholz, G., Dianov, G. L., Bécherel, O. J., & Lavin, M. F. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp359 · Cited by 95
Allinson, S. L., Dianova, I. I., & Dianov, G. L. (2003) · Acta Biochimica Polonica · doi:10.18388/abp.2003_3724 · Cited by 94
Human Proliferating Cell Nuclear Antigen, Poly(ADP-ribose) Polymerase-1, and p21 /
Frouin, I., Maga, G., Denegri, M., Riva, F., Savio, M., Spadari, S., Prosperi, E., & Scovassi, A. I. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.c300098200 · Cited by 93
Poly-ADP-ribose polymerase: Machinery for nuclear processes
Thomas, C. J., & Tulin, A. V. (2013) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2013.04.001 · Cited by 93
de Aguiar, P. H. N., Furtado, C., Repolês, B. M., Ribeiro, G. A., Mendes, I. C., Peloso, E. D. F., Gadelha, F. R., Macedo, A. M., Franco, G. R., Pena, S. D. J., et al. (2013) · PLoS neglected tropical diseases · doi:10.1371/journal.pntd.0002279 · Cited by 93
Quantitative characterization of protein–protein complexes involved in base excision DNA repair
Moor, N. A., Васильева, И. А., Anarbaev, R. O., Antson, A. A., & Lavrik, O. I. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv569 · Cited by 92
Xrcc1-dependent and Ku-dependent DNA double-strand break repair kinetics in Arabidopsis plants
Charbonnel, C., Gallego, M. E., & White, C. I. (2010) · The Plant Journal · doi:10.1111/j.1365-313x.2010.04331.x · Cited by 90
Regulation of the human poly(ADP-ribose) polymerase promoter by the ETS transcription factor
Soldatenkov, V. A., Albor, A., Patel, B. K. R., Dreszer, R., Dritschilo, A., & Notario, V. (1999) · Oncogene · doi:10.1038/sj.onc.1202778 · Cited by 90
Mosbaugh, D. W., & Linn, S. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)70197-5 · Cited by 88
DNA strand break repair and neurodegeneration
Rulten, S. L., & Caldecott, K. W. (2013) · DNA repair · doi:10.1016/j.dnarep.2013.04.008 · Cited by 85
Thompson, L. H., Brookman, K. W., Jones, N. J., Allen, S. A., & Carrano, A. V. (1990) · Molecular and Cellular Biology · doi:10.1128/mcb.10.12.6160-6171.1990 · Cited by 85
DNA-Induced Dimerization of Poly(ADP-ribose) Polymerase-1 Triggers Its Activation
Pion, E., Ullmann, G. M., Amé, J., Gérard, D., de MURCIA, G., & Bombarda, E. (2005) · Biochemistry · doi:10.1021/bi050755o · Cited by 84
Sano, Y., Date, H., Igarashi, S., Onodera, O., Oyake, M., Takahashi, T., Hayashi, S., Morimatsu, M., Takahashi, H., Makifuchi, T., et al. (2004) · Annals of Neurology · doi:10.1002/ana.10808 · Cited by 82
The novel human gene aprataxin is directly involved in DNA single-strand-break repair
Mosesso, P., Piane, M., Palitti, F., Pepe, G., Penna, S. C., & Chessa, L. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-004-4441-0 · Cited by 82
Thompson, L. H., Mooney, C. L., Burkhart-Schultz, K. J., Carrano, A. V., & Siciliano, M. J. (1985) · Somatic Cell and Molecular Genetics · doi:10.1007/bf01534738 · Cited by 79
Lebel, M., Lavoie, J., Gaudreault, I., Bronsard, M., & Drouin, R. (2003) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)64290-3 · Cited by 79
New directions in poly(ADP‐ribose) polymerase biology
Bock, F. J., & Chang, P. (2016) · FEBS Journal · doi:10.1111/febs.13737 · Cited by 78
Thompson, L. H., Bachinski, L. L., Stallings, R. L., Dolf, G., Weber, C. A., Westerveld, A., & Siciliano, M. J. (1989) · Genomics · doi:10.1016/0888-7543(89)90107-9 · Cited by 77
Ali, A. A. E., Jukes, R. M., Pearl, L. H., & Oliver, A. W. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkn1086 · Cited by 77
DNA single‐strand break repair is impaired in aprataxin‐related ataxia
Hirano, M., Yamamoto, A., Mori, T., Lan, L., Iwamoto, T., Aoki, M., Shimada, K., Furiya, Y., Kariya, S., Asai, H., et al. (2007) · Annals of Neurology · doi:10.1002/ana.21078 · Cited by 75
Oxidation state of the XRCC1 N-terminal domain regulates DNA polymerase β binding affinity
Cuneo, M. J., & London, R. E. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0914077107 · Cited by 74
Assignment of a human DNA-repair gene associated with sister-chromatid exchange to chromosome 19
Siciliano, M. J., Carrano, A. V., & Thompson, L. H. (1986) · Mutation Research Letters · doi:10.1016/0165-7992(86)90051-5 · Cited by 74
Mouse models of XRCC1 DNA repair polymorphisms and cancer
Ladiges, W. (2006) · Oncogene · doi:10.1038/sj.onc.1209370 · Cited by 73
Kutuzov, M. M., Khodyreva, S. N., Amé, J., Ilina, E. S., Sukhanova, M. V., Schreiber, V., & Lavrik, O. I. (2013) · Biochimie · doi:10.1016/j.biochi.2013.01.007 · Cited by 73
Progressive cerebellar atrophy and polyneuropathy: expanding the spectrum of PNKP mutations
Poulton, C. J., Oegema, R., Heijsman, D., Hoogeboom, J. A. M., Schot, R., Stroink, H., Willemsen, M. A. A. P., Verheijen, F. W., van der Spek, P. J., Kremer, A., et al. (2012) · Neurogenetics · doi:10.1007/s10048-012-0351-8 · Cited by 73
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
Beneke, R., Geisen, C., Zevnik, B., Bauch, T., Müller, W., Küpper, J., & Möröy, T. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.18.6695-6703.2000 · Cited by 71
Hanssen‐Bauer, A., Solvang‐Garten, K., Sundheim, O., Peña-Dı́az, J., Andersen, S. B., Slupphaug, G., Krokan, H. E., Wilson, D. M., Akbari, M., & Otterlei, M. (2011) · Environmental and Molecular Mutagenesis · doi:10.1002/em.20663 · Cited by 69
Self-citationStructural and Biophysical Studies of Human PARP-1 in Complex with Damaged DNA
Lilyestrom, W. G., van der Woerd, M. J., Clark, N., & Luger, K. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.11.062 · Cited by 69
Pinkel, D., Thompson, L. H., Gray, J. W., & Vanderlaan, M. (1985) · PubMed · Cited by 68
Zaniolo, K., Desnoyers, S., Leclerc, S., & Guérin, S. L. (2007) · BMC Molecular Biology · doi:10.1186/1471-2199-8-96 · Cited by 68
Repair of persistent strand breaks in the mitochondrial genome
Sýkora, P., Wilson, D. M., & Bohr, V. A. (2011) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2011.11.003 · Cited by 67
Self-citationDisruption 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
Engelward, B. P., Boosalis, M. S., J.Chen, B., Deng, Z., Siciliano, M. J., & Samson, L. D. (1993) · Carcinogenesis · doi:10.1093/carcin/14.2.175 · Cited by 66
Biophysical Characterization of Human XRCC1 and Its Binding to Damaged and Undamaged DNA
Mani, R. S., Karimi‐Busheri, F., Fanta, M., Caldecott, K. W., Cass, C. E., & Weinfeld, M. (2004) · Biochemistry · doi:10.1021/bi048615m · Cited by 66
Parp1–XRCC1 and the repair of DNA double strand breaks in mouse round spermatids
Ahmed, E. A., de Boer, P., Philippens, M. E. P., Kal, H. B., & de Rooij, D. G. (2009) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2009.10.011 · Cited by 66
Shimada, M., Dumitrache, L. C., Russell, H. R., & McKinnon, P. J. (2015) · The EMBO Journal · doi:10.15252/embj.201591363 · Cited by 66
The FHA domain of aprataxin interacts with the C-terminal region of XRCC1
Date, H., Igarashi, S., Sano, Y., Takahashi, T., Takahashi, T., Takano, H., Tsuji, S., Nishizawa, M., & Onodera, O. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.10.162 · Cited by 65
Rescue of Xrcc1 knockout mouse embryo lethality by transgene-complementation
Tebbs, R. S., Thompson, L. H., & Cleaver, J. E. (2003) · DNA repair · doi:10.1016/j.dnarep.2003.08.007 · Cited by 63
Huambachano, O., Herrera, F., Rancourt, A., & Satoh, M. S. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.175190 · Cited by 61
Single nucleotide polymorphisms in DNA repair genes and putative cancer risk
Köberle, B., Koch, B., Fischer, B., & Hartwig, A. (2016) · Archives of Toxicology · doi:10.1007/s00204-016-1771-2 · Cited by 61
The structural basis for partitioning of the XRCC1/DNA ligase III-α BRCT-mediated dimer complexes
Cuneo, M. J., Gabel, S. A., Krahn, J. M., Ricker, M. A., & London, R. E. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr419 · Cited by 61
Dillehay, L. E., Thompson, L. H., Minkler, J. L., & Carrano, A. V. (1983) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/0027-5107(83)90053-2 · Cited by 60
Wong, H., & Wilson, D. M. (2005) · Journal of Cellular Biochemistry · doi:10.1002/jcb.20448 · Cited by 59
Self-citationSaribasak, H., Maul, R. W., Cao, Z., McClure, R. L., Yang, W. W., McNeill, D. R., Wilson, D. M., & Gearhart, P. J. (2011) · The Journal of Experimental Medicine · doi:10.1084/jem.20111135 · Cited by 59
Self-citationMatsumoto, Y., Kim, K. M., & Bogenhagen, D. F. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.9.6187-6197.1994 · Cited by 59
Barrows, L. R., Holden, J. A., Anderson, M., & D’Arpa, P. (1998) · Mutation Research/DNA Repair · doi:10.1016/s0921-8777(98)00022-6 · Cited by 58
Structure and function of the DNA ligases encoded by the mammalian LIG3 gene
Tomkinson, A. E., & Sallmyr, A. (2013) · Gene · doi:10.1016/j.gene.2013.08.061 · Cited by 57
Pol β associated complex and base excision repair factors in mouse fibroblasts
Prasad, R., Williams, J. G., Hou, E. W., & Wilson, S. H. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks898 · Cited by 57
Uracil in DNA—Its biological significance
Oliński, R., Jurgowiak, M., & Zaremba, T. (2010) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2010.08.001 · Cited by 57
Kim, I.-K., Stegeman, R. A., Brosey, C. A., & Ellenberger, T. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.624718 · Cited by 57
Saffhill, R., & Ockey, C. H. (1985) · Chromosoma · doi:10.1007/bf00348697 · Cited by 56
Mammalian Base Excision Repair: Functional Partnership between PARP-1 and APE1 in AP-Site Repair
Prasad, R., Dyrkheeva, N. S., Williams, J. G., & Wilson, S. H. (2015) · PLoS ONE · doi:10.1371/journal.pone.0124269 · Cited by 56
Base Excision Repair Intermediates as Topoisomerase II Poisons
Wilstermann, A. M., & Osheroff, N. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105733200 · Cited by 55
Campalans, A., Moritz, E., Kortulewski, T., Biard, D. S. F., Epe, B., & Radicella, J. P. (2015) · Molecular and Cellular Biology · doi:10.1128/mcb.00134-15 · Cited by 55
Poly(ADP-ribosylation) of histones in intact human keratinocytes
Krupitza, G., & Cerutti, P. (1989) · Biochemistry · doi:10.1021/bi00435a063 · Cited by 55
Akbari, M., Solvang‐Garten, K., Hanssen‐Bauer, A., Lieske, N., Pettersen, H. S., Pettersen, G. K., Wilson, D. M., Krokan, H. E., & Otterlei, M. (2010) · DNA repair · doi:10.1016/j.dnarep.2010.04.002 · Cited by 54
Self-citationUse of mammalian DNA repair-deficient mutants to assess the effects of toxic metal compounds on DNA
Christie, N. T., Cantoni, O., Evans, R. M., Meyn, R. E., & Costa, M. (1984) · Biochemical Pharmacology · doi:10.1016/0006-2952(84)90289-2 · Cited by 54
Berghammer, H., Ebner, M., Marksteiner, R., & Auer, B. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00448-2 · Cited by 53
Suzuki, H., Uchida, K., Shima, H., Sato, T., Okamoto, T., Kimura, T., & Miwa, M. (1987) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(87)90543-2 · Cited by 53
Churchill, M. E., Peak, J. G., & Peak, M. J. (1991) · Photochemistry and Photobiology · doi:10.1111/j.1751-1097.1991.tb03927.x · Cited by 52
vanAnkeren, S. C., Murray, D. J., & Meyn, R. E. (1988) · Radiation Research · doi:10.2307/3577393 · Cited by 52
Mani, R. S., Fanta, M., Karimi‐Busheri, F., Silver, E. T., Virgen, C. A., Caldecott, K. W., Cass, C. E., & Weinfeld, M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704867200 · Cited by 50
Recovery from Sublethal and Potentially Lethal Damage in an X-Ray-Sensitive CHO Cell
Schwartz, J. L., Giovanazzi, S. M., & Weichselbaum, R. R. (1987) · Radiation Research · doi:10.2307/3577021 · Cited by 49
Base excision repair capacity in informing healthspan
Brenerman, B. M., Illuzzi, J. L., & Wilson, D. M. (2014) · Carcinogenesis · doi:10.1093/carcin/bgu225 · Cited by 49
Self-citationLi, S., Kanno, S.-I., Watanabe, R., Ogiwara, H., Kohno, T., Watanabe, G., Yasui, A., & Lieber, M. R. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.287797 · Cited by 48
Structural studies of the PARP-1 BRCT domain
Loeffler, P. A., Cuneo, M. J., Mueller, G. A., DeRose, E. F., Gabel, S. A., & London, R. E. (2011) · BMC Structural Biology · doi:10.1186/1472-6807-11-37 · Cited by 48
Carrano, A. V., Minkler, J. L., Dillehay, L. E., & Thompson, L. H. (1986) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/0027-5107(86)90090-4 · Cited by 46
Mapping of the Interaction Interface of DNA Polymerase β with XRCC1
Gryk, M. R., Marintchev, A., Maciejewski, M. W., Robertson, A., Wilson, S. H., & Mullen, G. P. (2002) · Structure · doi:10.1016/s0969-2126(02)00908-5 · Cited by 45
Coordination of DNA repair by NEIL1 and PARP-1: a possible link to aging
Noren Hooten, N., Fitzpatrick, M., Kompaniez, K., Jacob, K. D., Moore, B. R., Nagle, J., Barnes, J., Lohani, A., & Evans, M. K. (2012) · Aging · doi:10.18632/aging.100492 · Cited by 44 · cited 6×
“The physical association of PARP1 with these DNA glycosylases has been proposed to play a role in aging, given that the NEIL1-PARP1 interaction declines with age in a murine model [106].”
BackgroundInfluentialDNA-Mediated Transfer of a Human DNA Repair Gene That Controls Sister Chromatid Exchange
Thompson, L. H., Brookman, K. W., Minkler, J. L., Fuscoe, J. C., Henning, K. A., & Carrano, A. V. (1985) · Molecular and Cellular Biology · doi:10.1128/mcb.5.4.881 · Cited by 44
Preventing oxidation of cellular XRCC1 affects PARP-mediated DNA damage responses
Horton, J. K., Stefanick, D. F., Gassman, N. R., Williams, J. G., Gabel, S. A., Cuneo, M. J., Prasad, R., Kedar, P. S., DeRose, E. F., Hou, E. W., et al. (2013) · DNA repair · doi:10.1016/j.dnarep.2013.06.004 · Cited by 43
Lebedeva, N. A., Rechkunova, N. I., Ishchenko, A. A., Saparbaev, M. K., & Lavrik, O. I. (2013) · DNA repair · doi:10.1016/j.dnarep.2013.09.008 · Cited by 43
Herzog, H., Zabel, B. U., Schneider, R., Auer, B., Hirsch‐Kauffmann, M., & Schweiger, M. R. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.10.3514 · Cited by 42
Cantoni, O., Murray, D. L., & Meyn, R. E. (1987) · Chemico-Biological Interactions · doi:10.1016/0009-2797(87)90102-5 · Cited by 41
DNA Damage Levels and Biochemical Repair Capacities Associated with XRCC1 Deficiency
Wong, H., Kim, D., Hogue, B. A., McNeill, D. R., & Wilson, D. M. (2005) · Biochemistry · doi:10.1021/bi051161o · Cited by 41
Self-citationHuman Nuclear NAD + ADP-Ribosyltransferase(polymerizing): Organization of the Gene
Auer, B., Nagl, U. O., Herzog, H., Schneider, R., & Schweiger, M. (1989) · DNA · doi:10.1089/dna.1989.8.575 · Cited by 39
Keith, G., Desgrès, J., & de MURCIA, G. (1990) · Analytical Biochemistry · doi:10.1016/0003-2697(90)90224-w · Cited by 39
Kim, J. W., Kim, K., Kang, K.-W., & Joe, C. O. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.11.8121 · Cited by 38
Fan, J., Wilson, P. F., Wong, H., Urbin, S. S., Thompson, L. H., & Wilson, D. M. (2007) · Environmental and Molecular Mutagenesis · doi:10.1002/em.20312 · Cited by 36
Self-citationXRCC1 protects against the lethality of induced oxidative DNA damage in nondividing neural cells
Kulkarni, A., McNeill, D. R., Gleichmann, M., Mattson, M. P., & Wilson, D. M. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkn480 · Cited by 36
Self-citationMarintchev, A. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg159 · Cited by 35
DNA Strand Break-Mediated Partitioning of Poly(ADP-Ribose) Polymerase Function
Panzeter, P. L., & Althaus, F. R. (1994) · Biochemistry · doi:10.1021/bi00198a028 · Cited by 34
Domı́nguez, I., Daza, P., Natarajan, A. T., & Cortés, F. (1998) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/s0027-5107(97)00241-8 · Cited by 33
Human poly(ADP‐ribose) polymerase gene
Yokoyama, Y., Kawamoto, T., Mitsuuchi, Y., Kurosaki, T., Toda, K., Ushiro, H., Terashima, M., Sumimoto, H., Kuribayashi, I., Yamamoto, Y., et al. (1990) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1990.tb15647.x · Cited by 32
Della-Maria, J., Hegde, M. L., McNeill, D. R., Matsumoto, Y., Tsai, M.-S., Ellenberger, T., Wilson, D. M., MITRA, S. P., & Tomkinson, A. E. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.369975 · Cited by 31
Self-citationPoly(ADP-ribosyl)ation of chromatin in an in-vitro poly(ADP-ribose)-turnover system
Thomassin, H., Ménard, L., Hengartner, C. J., Kirkland, J. B., & Poirier, G. G. (1992) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/0167-4889(92)90199-l · Cited by 30
Hassler, M., & Ladurner, A. G. (2012) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2012.08.005 · Cited by 30
McNeill, D. R., Lin, P., Miller, M. G., Pistell, P. J., de Souza-Pinto, N. C., Fishbein, K. W., Spencer, R. G. S., Liu, Y., Pettan-Brewer, C., Ladiges, W., et al. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr280 · Cited by 29
Self-citationLü, M., Mani, R. S., Karimi‐Busheri, F., Fanta, M., Wang, H., Litchfeld, D. W., & Weinfeld, M. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp1023 · Cited by 29
Assignment of the gene encoding DNA ligase I to human chromosome 19q13.2–13.3
Barnes, D. E., Kodama, K., Tynan, K., Trask, B. J., Christensen, M. L., de Jong, P. J., Spurr, N. K., Lindahl, T. L., & Mohrenweiser, H. W. (1992) · Genomics · doi:10.1016/0888-7543(92)90422-o · Cited by 27
Parsons, J. L., Dianova, I. I., Boswell, E. J., Weinfeld, M., & Dianov, G. L. (2005) · FEBS Journal · doi:10.1111/j.1742-4658.2005.04962.x · Cited by 26
Characterization of the interactions of PARP-1 with UV-damaged DNA in vivo and in vitro
Purohit, N. K., Robu, M., Shah, R. G., Geacintov, N. E., & Shah, G. M. (2016) · Scientific Reports · doi:10.1038/srep19020 · Cited by 26
Laniel, M., Bergeron, M., Poirier, G. G., & Guérin, S. L. (1997) · Biochemistry and Cell Biology · doi:10.1139/bcb-75-4-427 · Cited by 25
Pacini, A., Quattrone, A., Denegri, M., Fiorillo, C., Nediani, C., y Cajal, S. R., & Nassi, P. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.49.35107 · Cited by 24
Belle, M. L., Linn, S., & Thompson, L. H. (1984) · Mutation Research Letters · doi:10.1016/0165-7992(84)90035-6 · Cited by 24
Laniel, M., & Guérin, S. L. (1997) · Biochemistry and Cell Biology · doi:10.1139/o97-051 · Cited by 22
DNA polymerase β-dependent cell survival independent of XRCC1 expression
Horton, J. K., Gassman, N. R., Dunigan, B. D., Stefanick, D. F., & Wilson, S. H. (2014) · DNA repair · doi:10.1016/j.dnarep.2014.11.008 · Cited by 21
Ghosh, S., Canugovi, C., Yoon, J. S., Wilson, D. M., Croteau, D. L., Mattson, M. P., & Bohr, V. A. (2015) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2015.04.004 · Cited by 20
Self-citationPotvin, F., Thibodeau, J., Kirkland, J. B., Dandenault, B., Duchaine, C., & Poirier, G. G. (1992) · FEBS Letters · doi:10.1016/0014-5793(92)80457-r · Cited by 18
PARP-2: Structure-Function Relationship
Schreiber, V., Ricoul, M., Amé, J., Dantzer, F., Meder, V., Spenlehauer, C., Stiegler, P., Niedergang, C., Sabatier, L., Favaudon, V., et al. (2006) · Springer eBooks · doi:10.1007/0-387-36005-0_2 · Cited by 17
Maldonado, A., Hernández, P., & Gutiérrez, C. (1985) · Experimental Cell Research · doi:10.1016/0014-4827(85)90501-4 · Cited by 17
Ray, J. H., Louie, E., & German, J. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.8.2368 · Cited by 15
Poly(ADP-ribose) catabolism in mammalian cells
Lagueux, J., Shah, G. M., Ménard, L., Thomassin, H., Duchaine, C., Hengartner, C. J., & Poirier, G. G. (1994) · Springer eBooks · doi:10.1007/978-1-4615-2614-8_6 · Cited by 13
Lebedeva, N. A., Anarbaev, R. O., Sukhanova, M. V., Васильева, И. А., Rechkunova, N. I., & Lavrik, O. I. (2015) · Bioscience Reports · doi:10.1042/bsr20140192 · Cited by 13
Laniel, M., Poirier, G. G., & Guérin, S. L. (2004) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/j.bbaexp.2004.04.003 · Cited by 12
SNF2H interacts with XRCC1 and is involved in repair of H2O2-induced DNA damage
Kubota, Y., Shimizu, S., Yasuhira, S., & Horiuchi, S. (2016) · DNA repair · doi:10.1016/j.dnarep.2016.03.010 · Cited by 11
DNA-Mediated Transfer of a Human DNA Repair Gene That Controls Sister Chromatid Exchange
Thompson, L. H., Brookman, K. W., Minkler, J. L., et al. (1985) · Molecular and Cellular Biology · doi:10.1128/mcb.5.4.881-884.1985 · Cited by 9
Poly(ADP-ribose) catabolism in mammalian cells
Lagueux, J., Shah, G. M., M�nard, L., Thomassin, H., Duchaine, C., Hengartner, C. J., & Poirier, G. G. (1994) · Molecular and Cellular Biochemistry · doi:10.1007/bf00928442 · Cited by 9
Research works printed but not linked: 1
- Li, 2013, Major Human Apurinic/Apyrimidinic Endonuclease, APE1, Antioxid. Redox Signal
Cited by
Sorted by citations
Huang, R., & Zhou, P. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00648-7 · Cited by 1,015
Doxorubicin—An Agent with Multiple Mechanisms of Anticancer Activity
Kciuk, M., Gielecińska, A., Mujwar, S., Kołat, D., Kałuzińska‐Kołat, Ż., Çeli̇k, İ., & Kontek, R. (2023) · Cells · doi:10.3390/cells12040659 · Cited by 906
Relationships among smoking, oxidative stress, inflammation, macromolecular damage, and cancer
Caliri, A. W., Tommasi, S., & Nia, A. B. (2021) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2021.108365 · Cited by 750
Chronic inflammation and the hallmarks of aging
Baechle, J. J., Chen, N., Makhijani, P., Winer, S., Furman, D., & Winer, D. A. (2023) · Molecular Metabolism · doi:10.1016/j.molmet.2023.101755 · Cited by 471
RNA-binding proteins in tumor progression
Qin, H., Ni, H., Liu, Y., Yuan, Y., Xi, T., Li, X., & Zheng, L. (2020) · Journal of Hematology & Oncology · doi:10.1186/s13045-020-00927-w · Cited by 387
Metadata
- Authors
- Abbotts, R., & Wilson, D. M.
- Affiliations
- National Institutes of Health (US)
- Corresponding author
- Wilson, David M.
- Venue
- Free Radical Biology and Medicine
- Publisher
- Elsevier BV
- Published
- 2017-06
- Volume
- 107
- Pages
- 228-244
- ISSN
- 0891-5849 (ISSN-L)
- PMC
- PMC5443707
- OpenAlex
- W2553815939
- Cited by
- 240
- References
- 318
- Citations by year
- 2026: 9 · 2025: 22 · 2024: 25 · 2023: 31 · 2022: 32 · 2021: 41 · 2020: 31 · 2019: 23 · 2018: 18 · 2017: 8
- FWCI
- 1.46
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Free Radical Biology and Medicine (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health
- National Institute on Aging (ZIAAG000751)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Health Sciences › Medicine › Oncology › PARP inhibition in cancer therapy
- Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Effects of Radiation Exposure
- Keywords
- single-strand breaks, PARP1, XRCC1, DNA damage, reactive oxygen species, abasic sites, DNA cross-links, base lesions, endogenous DNA damage, meiotic recombination, class switch recombination
- MeSH terms
- Poly (ADP-Ribose) Polymerase-1, X-ray Repair Cross Complementing Protein 1, Animals, Benzopyrenes, DNA Damage, DNA Repair, Humans, Nervous System Diseases, Radiation, Ionizing, Sunlight, Reactive Oxygen Species, DNA Breaks, Single-Stranded
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review