Coordination of DNA single strand break repair

How mitochondria produce reactive oxygen species

Murphy, M. P. (2009) · Biochemical Journal · doi:10.1042/bj20081386 · Cited by 8,207 · 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

Genome maintenance mechanisms for preventing cancer

Hoeijmakers, J. H. J. (2001) · Nature · doi:10.1038/35077232 · Cited by 3,939 · see citing works

Mitochondria and cancer

Wallace, D. C. (2012) · Nature Reviews Cancer · doi:10.1038/nrc3365 · Cited by 2,404 · see citing works

Cellular roles of DNA topoisomerases: a molecular perspective

Wang, J. C. (2002) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm831 · Cited by 2,364 · see citing works

Topoisomerase I inhibitors: camptothecins and beyond

Pommier, Y. G. (2006) · Nature reviews. Cancer · doi:10.1038/nrc1977 · Cited by 2,295 · see citing works

Poly(ADP-ribose): novel functions for an old molecule

Schreiber, V., Dantzer, F., Amé, J., & de MURCIA, G. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1963 · Cited by 1,917 · see citing works

Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions

D’Amours, D., Desnoyers, S., D’Silva, I., & Poirier, G. G. (1999) · Biochemical Journal · doi:10.1042/bj3420249 · Cited by 1,819 · see citing works

Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria

Turrens, J. F., & Boveris, A. (1980) · Biochemical Journal · doi:10.1042/bj1910421 · Cited by 1,601 · see citing works

Role of poly(ADP-ribose) formation in DNA repair

Satoh, M. S., & Lindahl, T. L. (1992) · Nature · doi:10.1038/356356a0 · Cited by 1,181 · see citing works

Endogenous DNA damage in humans: a review of quantitative data

Bont, R. D. (2004) · Mutagenesis · doi:10.1093/mutage/geh025 · Cited by 1,065 · see citing works

Requirement of poly(ADP-ribose) polymerase in recovery from DNA damage in mice and in cells

Murcia, J. M., Niedergang, C., Trucco, C., Ricoul, M., Dutrillaux, B., Mark, M. P., Oliver, F. J., Masson, M., Dierich, A., LeMeur, M., et al. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.14.7303 · Cited by 1,058 · see citing works

Arrest of replication forks by drug-stabilized topoisomerase I-DNA cleavable complexes as a mechanism of cell killing by camptothecin.

Hsiang, Y. H., Lihou, M. G., & Liu, L. F. (1989) · PubMed · Cited by 1,027 · see citing works

Oxidative Strand Scission of Nucleic Acids:  Routes Initiated by Hydrogen Abstraction from the Sugar Moiety

Pogozelski, W. K., & Tullius, T. D. (1998) · Chemical Reviews · doi:10.1021/cr960437i · Cited by 1,018 · see citing works

Free radical-induced damage to DNA: mechanisms and measurement

Dizdaroglu, M., Jaruga, P., Birincioglu, M., & Rodriguez, H. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00826-2 · Cited by 953 · see citing works

ATR prohibits replication catastrophe by preventing global exhaustion of RPA

Toledo, L. I., Altmeyer, M., Rask, M.-B., Lukas, C., Larsen, D. H., Povlsen, L. K., Bekker-Jensen, S., Mailand, N., Bartek, J., & Lukas, J. (2013) · Cell · doi:10.1016/j.cell.2013.10.043 · Cited by 911 · see citing works

XRCC1 Is Specifically Associated with Poly(ADP-Ribose) Polymerase and Negatively Regulates Its Activity following DNA Damage

Masson, M., Niedergang, C., Schreiber, V., Muller, S., Murcia, J. M., & de MURCIA, G. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.6.3563 · Cited by 910 · 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

MUTAGENESIS BY APURINIC/APYRIMIDINIC SITES

Loeb, L. A., & Preston, B. D. (1986) · Annual Review of Genetics · doi:10.1146/annurev.ge.20.120186.001221 · Cited by 901 · see citing works

A Pathway of Double-Strand Break Rejoining Dependent upon ATM, Artemis, and Proteins Locating to γ-H2AX Foci

Riballo, E., Kühne, M., Rief, N., Doherty, A., Smith, G. C. M., Recio, M.-J., Reis, C., Dahm, K., Fricke, A., Krempler, A., et al. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.10.029 · Cited by 837 · see citing works

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 · see citing works

Poly(ADP-ribosyl)ation by PARP-1: `PAR-laying' NAD + into a nuclear signalPreprint

Kim, M. Y., Zhang, T., & Kraus, W. L. (2005) · Genes & Development · doi:10.1101/gad.1331805 · Cited by 803 · see citing works

Mutagenic deamination of cytosine residues in DNA

Duncan, B. K., & Miller, J. H. (1980) · Nature · doi:10.1038/287560a0 · Cited by 792 · see citing works

Second pathway for completion of human DNA base excision‐repair: reconstitution with purified proteins and requirement for DNase IV (FEN1)

Klungland, A., & Lindahl, T. (1997) · The EMBO Journal · doi:10.1093/emboj/16.11.3341 · Cited by 789 · see citing works

Reconstitution of DNA base excision‐repair with purified human proteins: interaction between DNA polymerase beta and the XRCC1 protein.

Kubota, Y., Nash, R. A., Klungland, A., Schär, P., Barnes, D. E., & Lindahl, T. L. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb01056.x · Cited by 776 · see citing works

Mice lacking ADPRT and poly(ADP-ribosyl)ation develop normally but are susceptible to skin disease.Preprint

Wang, Z. Q., Auer, B., Stingl, L., Berghammer, H., Haidacher, D., Schweiger, M. R., & Wagner, E. F. (1995) · Genes & Development · doi:10.1101/gad.9.5.509 · Cited by 774 · see citing works

A superfamily of conserved domains in DNA damage‐ responsive cell cycle checkpoint proteins

Bork, P., Hofmann, K., Bucher, P., Neuwald, A. F., Altschul, S. F., & Koonin, E. V. (1997) · The FASEB Journal · doi:10.1096/fasebj.11.1.9034168 · Cited by 746 · see citing works

PARP-2, A Novel Mammalian DNA Damage-dependent Poly(ADP-ribose) Polymerase

Amé, J., Rolli, V., Schreiber, V., Niedergang, C., Apiou, F., Decker, P., Muller, S., Höger, T. H., Murcia, J. M., & de MURCIA, G. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.25.17860 · Cited by 744 · see citing works

Involvement of Poly(ADP-ribose) Polymerase-1 and XRCC1/DNA Ligase III in an Alternative Route for DNA Double-strand Breaks Rejoining

Audebert, M., Salles, B., & Calsou, P. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404524200 · Cited by 709 · see citing works

Poly(ADP-ribose) Polymerase-2 (PARP-2) Is Required for Efficient Base Excision DNA Repair in Association with PARP-1 and XRCC1

Schreiber, V., Amé, J., Dollé, P., Schultz, I., Rinaldi, B., Fraulob, V., Murcia, J. M., & de MURCIA, G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202390200 · Cited by 706 · see citing works

DNA repair mechanisms in dividing and non-dividing cells

Iyama, T., & Wilson, D. M. (2013) · DNA Repair · doi:10.1016/j.dnarep.2013.04.015 · Cited by 697 · see citing works

Excision of Deoxyribose Phosphate Residues by DNA Polymerase β During DNA Repair

Matsumoto, Y., & Kim, K. (1995) · Science · doi:10.1126/science.7624801 · Cited by 683 · see citing works

Structural Basis for DNA Damage–Dependent Poly(ADP-ribosyl)ation by Human PARP-1

Langelier, M.-F., Planck, J. L., Roy, S., & Pascal, J. M. (2012) · Science · doi:10.1126/science.1216338 · Cited by 669 · see citing works

A requirement for PARP-1 for the assembly or stability of XRCC1 nuclear foci at sites of oxidative DNA damage

El‐Khamisy, S. F. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg761 · Cited by 660 · see citing works

Nicotinamide mononucleotide activation of a new DNA-dependent polyadenylic acid synthesizing nuclear enzyme

Chambon, P., Weill, J. D., & Mandel, P. (1963) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(63)90024-x · Cited by 654 · see citing works

Functional interaction between PARP‐1 and PARP‐2 in chromosome stability and embryonic development in mouse

Murcia, J. M., Ricoul, M., Tartier, L., Niedergang, C., Huber, A., Dantzer, F., Schreiber, V., Amé, J., Dierich, A., LeMeur, M., et al. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg206 · Cited by 629 · see citing works

XRCC1 Polypeptide Interacts with DNA Polymerase and Possibly Poly (ADP-Ribose) Polymerase, and DNA Ligase III Is a Novel Molecular 'Nick-Sensor' In Vitro

Caldecott, K. W., Aoufouchi, S., Johnson, P., & Shall, S. (1996) · Nucleic Acids Research · doi:10.1093/nar/24.22.4387 · Cited by 620 · see citing works

DNA polymerases and cancer

Lange, S. S., Takata, K.-I., & Wood, R. D. (2011) · Nature Reviews Cancer · doi:10.1038/nrc2998 · Cited by 615 · see citing works

XRCC1 Stimulates Human Polynucleotide Kinase Activity at Damaged DNA Termini and Accelerates DNA Single-Strand Break Repair

Whitehouse, C. J., Taylor, R., Thistlethwaite, A., Zhang, H., Karimi‐Busheri, F., Lasko, D. D., Weinfeld, M., & Caldecott, K. W. (2001) · Cell · doi:10.1016/s0092-8674(01)00195-7 · Cited by 608 · see citing works

An N -Glycosidase from Escherichia coli That Releases Free Uracil from DNA Containing Deaminated Cytosine Residues

Lindahl, T. L. (1974) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.71.9.3649 · Cited by 605 · see citing works

XRCC1 and DNA strand break repair

Caldecott, K. W. (2003) · DNA repair · doi:10.1016/s1568-7864(03)00118-6 · Cited by 598 · see citing works

Poly (ADP-Ribose) and ADP-Ribosylation of Proteins

Hayaishi, O., & Veda, K. (1977) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.46.070177.000523 · Cited by 585 · see citing works

Poly ADP-ribose and ADP-ribosylation of proteins

Hayaishi, O. (1976) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(76)90255-3 · Cited by 573 · see citing works

PARP is important for genomic stability but dispensable in apoptosisPreprint

Wang, Z., Stingl, L., Morrison, C. G., Jantsch, M. F., Łoś, M., Schulze‐Osthoff, K., & Wagner, E. F. (1997) · Genes & Development · doi:10.1101/gad.11.18.2347 · Cited by 557 · see citing works

Transcription initiation from TATA-less promoters within eukaryotic protein-coding genes

Smale, S. T. (1997) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/s0167-4781(96)00206-0 · Cited by 540 · see citing works

Poly(ADP-ribose) Binds to Specific Domains in DNA Damage Checkpoint Proteins

Pleschke, J. M., Kleczkowska, H. E., Strohm, M., & Althaus, F. R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m006520200 · Cited by 537 · see citing works

Mutation of TDP1, encoding a topoisomerase I–dependent DNA damage repair enzyme, in spinocerebellar ataxia with axonal neuropathy

Takashima, H., Boerkoel, C. F., John, J., Saifi, G. M., Salih, M. A. M., Armstrong, D., Mao, Y., Quiocho, F. A., Roa, B. B., Nakagawa, M., et al. (2002) · Nature Genetics · doi:10.1038/ng987 · Cited by 522 · see citing works

An Overview of Chemical Processes That Damage Cellular DNA: Spontaneous Hydrolysis, Alkylation, and Reactions with Radicals

Gates, K. S. (2009) · Chemical Research in Toxicology · doi:10.1021/tx900242k · Cited by 509 · see citing works

Base Excision Repair Is Impaired in Mammalian Cells Lacking Poly(ADP-ribose) Polymerase-1

Dantzer, F., de la Rubia, G., Murcia, J. M., Hostomský, Z., de MURCIA, G., & Schreiber, V. (2000) · Biochemistry · doi:10.1021/bi0003442 · Cited by 505 · see citing works

An interaction between the mammalian DNA repair protein XRCC1 and DNA ligase III

Caldecott, K. W., McKeown, C., Tucker, J. D., Ljungquist, S., & Thompson, L. H. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.1.68 · Cited by 504 · see citing works

Poly(ADP-ribose) synthesis in vitro programmed by damaged DNA. A comparison of DNA molecules containing different types of strand breaks.

Benjamin, R. C., & Gill, D. M. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)70491-8 · Cited by 489 · see citing works

Poly(ADP-ribose) (PAR) binding to apoptosis-inducing factor is critical for PAR polymerase-1-dependent cell death (parthanatos)

Wang, Y., Kim, N. S., Haince, J.-F., Kang, H. C., David, K. K., Andrabi, S. A., Poirier, G. G., Dawson, V. L., & Dawson, T. M. (2011) · Science Signaling · doi:10.1126/scisignal.2000902 · Cited by 476 · see citing works

AP Endonuclease-Independent DNA Base Excision Repair in Human Cells

Wiederhold, L. R., Leppard, J. B., Kedar, P. S., Karimi‐Busheri, F., Rasouli‐Nia, A., Weinfeld, M., Tomkinson, A. E., Izumi, T., Prasad, R., Wilson, S. H., et al. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.06.003 · Cited by 472 · see citing works

Crystal Structure of Rat DNA Polymerase β: Evidence for a Common Polymerase Mechanism

Sawaya, M. R., Pelletier, H., Kumar, A., Wilson, S. H., & Kraut, J. (1994) · Science · doi:10.1126/science.7516581 · Cited by 469 · see citing works

XRCC1 coordinates the initial and late stages of DNA abasic site repair through protein–protein interactions

Vidal, A. E., Boiteux, S., Hickson, I. D., & Radicella, J. P. (2001) · The EMBO Journal · doi:10.1093/emboj/20.22.6530 · Cited by 459 · see citing works

XRCC1 keeps DNA from getting stranded

Thompson, L. H., & West, M. G. (2000) · Mutation Research/DNA Repair · doi:10.1016/s0921-8777(99)00058-0 · Cited by 444 · see citing works

A unified view of base excision repair: Lesion-dependent protein complexes regulated by post-translational modification

Almeida, K. H., & Sobol, R. W. (2007) · DNA Repair · doi:10.1016/j.dnarep.2007.01.009 · Cited by 437 · see citing works

The gene mutated in ataxia-ocular apraxia 1 encodes the new HIT/Zn-finger protein aprataxin

Moreira, M.-C., Barbot, C., Tachi, N., Kozuka, N., Uchida, E., Gibson, T. J., Mendonça, P., Costa, M. M. R., Barros, J., Yanagisawa, T., et al. (2001) · Nature Genetics · doi:10.1038/ng1001-189 · Cited by 434 · see citing works

Poly(ADP-ribose)-binding zinc finger motifs in DNA repair/checkpoint proteins

Ahel, I., Ahel, D., Matsusaka, T., Clark, A. J., Pines, J., Boulton, S. J., & West, S. C. (2008) · Nature · doi:10.1038/nature06420 · Cited by 429 · see citing works

Defective DNA single-strand break repair in spinocerebellar ataxia with axonal neuropathy-1

El‐Khamisy, S. F., Saifi, G. M., Weinfeld, M., Johansson, F., Helleday, T., Lupski, J. R., & Caldecott, K. W. (2005) · Nature · doi:10.1038/nature03314 · Cited by 426 · see citing works

Sister Chromatid Exchanges Are Mediated by Homologous Recombination in Vertebrate Cells

Sonoda, E., Sasaki, M. S., Morrison, C. G., Yamaguchi‐Iwai, Y., Takata, M., & Takeda, S. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.7.5166 · Cited by 426 · see citing works

A eukaryotic enzyme that can disjoin dead-end covalent complexes between DNA and type I topoisomerases.

Yang, S., Burgin, A. B., Huizenga, B. N., Robertson, C. A., Yao, K. C., & Nash, H. A. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.21.11534 · Cited by 413 · see citing works

Nonenzymatic methylation of DNA by the intracellular methyl group donor S‐adenosyl‐L‐methionine is a potentially mutagenic reaction.

Rydberg, B., & Lindahl, T. L. (1982) · The EMBO Journal · doi:10.1002/j.1460-2075.1982.tb01149.x · Cited by 410 · see citing works

DNA glycosylases: In DNA repair and beyond

Jacobs, A. L., & Schär, P. (2012) · Chromosoma · doi:10.1007/s00412-011-0347-4 · Cited by 407 · see citing works

Single-strand interruptions in replicating chromosomes cause double-strand breaks

Kuzminov, A. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.131009198 · Cited by 407 · see citing works

Molecular Cloning of the Human XRCC1 Gene, Which Corrects Defective DNA Strand Break Repair and Sister Chromatid Exchange

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 · Cited by 404 · see citing works

A Central Role for DNA Replication Forks in Checkpoint Activation and Response

Tercero, J. A., Longhese, M. P., & Diffley, J. F. X. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00169-2 · Cited by 394 · see citing works

Early-onset ataxia with ocular motor apraxia and hypoalbuminemia is caused by mutations in a new HIT superfamily gene

Date, H., Onodera, O., Tanaka, H., Iwabuchi, K., Uekawa, K., Igarashi, S., Koike, R., Hiroi, T., Yuasa, T., Awaya, Y., et al. (2001) · Nature Genetics · doi:10.1038/ng1001-184 · Cited by 386 · see citing works

The structure and catalytic mechanism of a poly(ADP-ribose) glycohydrolase

Slade, D., Dunstan, M. S., Barkauskaite, E., Weston, R., Lafite, P., Dixon, N., Ahel, M., Leys, D., & Ahel, I. (2011) · Nature · doi:10.1038/nature10404 · Cited by 385 · see citing works

The neurodegenerative disease protein aprataxin resolves abortive DNA ligation intermediates

Ahel, I., Rass, U., El‐Khamisy, S. F., Katyal, S., Clements, P. M., McKinnon, P. J., Caldecott, K. W., & West, S. C. (2006) · Nature · doi:10.1038/nature05164 · Cited by 383 · see citing works

ADP-ribosylation in mammalian cell ghosts. Dependence of poly(ADP-ribose) synthesis on strand breakage in DNA.

Benjamin, R. C., & Gill, D. M. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)70490-6 · Cited by 379 · see citing works

Conversion of Topoisomerase I Cleavage Complexes on the Leading Strand of Ribosomal DNA into 5′-Phosphorylated DNA Double-Strand Breaks by Replication Runoff

Strumberg, D., Pilon, A. A., Smith, M. W., Hickey, R. J., Malkas, L. H., & Pommier, Y. G. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.11.3977-3987.2000 · Cited by 367 · see citing works

Formation and repair of oxidatively generated damage in cellular DNA

Cadet, J., Davies, K. J. A., de Medeiros, M. H. G., Mascio, P. D., & Wagner, J. R. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.12.049 · Cited by 356 · see citing works

DNA repair defect in poly(ADP-ribose) polymerase-deficient cell lines

Trucco, C. (1998) · Nucleic Acids Research · doi:10.1093/nar/26.11.2644 · Cited by 348 · see citing works

Tyrosyl-DNA-phosphodiesterases (TDP1 and TDP2)

Pommier, Y. G., Huang, S.-Y. N., Gao, R., Das, B. B., Murai, J., & Marchand, C. (2014) · DNA repair · doi:10.1016/j.dnarep.2014.03.020 · Cited by 341 · see citing works

Post‐replicative base excision repair in replication foci

Otterlei, M., Warbrick, E., Nagelhus, T. A., Haug, T., Slupphaug, G., Akbari, M., Aas, P. A., Steinsbekk, K., Bakke, O., & Krokan, H. E. (1999) · The EMBO Journal · doi:10.1093/emboj/18.13.3834 · Cited by 340 · see citing works

RNase H2-Initiated Ribonucleotide Excision Repair

Sparks, J. L., Chon, H., Cerritelli, S. M., Kunkel, T. A., Johansson, E., Crouch, R. J., & Burgers, P. M. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.06.035 · Cited by 339 · see citing works

Failure to degrade poly(ADP-ribose) causes increased sensitivity to cytotoxicity and early embryonic lethality

Koh, D. W., Lawler, A. M., Poitras, M. F., Sasaki, M., Wattler, S., Nehls, M. C., Stöger, T., Poirier, G. G., Dawson, V. L., & Dawson, T. M. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0406182101 · Cited by 339 · see citing works

Oxidative DNA damage & repair: An introduction

Cadet, J., & Davies, K. J. A. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.03.030 · Cited by 339 · see citing works

Requirement for theXrcc1DNA Base Excision Repair Gene during Early Mouse Development

Tebbs, R. S., Flannery, M. L., Meneses, J. J., Hartmann, A., Tucker, J. D., Thompson, L. H., Cleaver, J. E., & Pedersen, R. A. (1999) · Developmental Biology · doi:10.1006/dbio.1999.9232 · Cited by 337 · see citing works

Involvement of XRCC1 and DNA Ligase III Gene Products in DNA Base Excision Repair

Cappelli, E., Taylor, R., Cevasco, M., Abbondandolo, A., Caldecott, K. W., & Fròsina, G. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.38.23970 · Cited by 333 · see citing works

The Protein Kinase CK2 Facilitates Repair of Chromosomal DNA Single-Strand Breaks

Loizou, J. I., El‐Khamisy, S. F., Zlatanou, A., Moore, D. J., Chan, D. W., Qin, J., Sarno, S., Meggio, F., Pinna, L. A., & Caldecott, K. W. (2004) · Cell · doi:10.1016/s0092-8674(04)00206-5 · Cited by 330 · see citing works

A family of macrodomain proteins reverses cellular mono-ADP-ribosylation

Jankevicius, G., Hassler, M., Golia, B., Rybin, V., Zacharias, M., Timinszky, G., & Ladurner, A. G. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2523 · Cited by 330 · see citing works

Molecular mechanism of poly(ADP-ribosyl)ation by PARP1 and identification of lysine residues as ADP-ribose acceptor sites

Altmeyer, M., Messner, S., Hassa, P. O., Fey, M., & Hottiger, M. O. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp229 · Cited by 325 · see citing works

DNA repair deficiency and neurological disease

McKinnon, P. J. (2009) · Nature Reviews Neuroscience · doi:10.1038/nrn2559 · Cited by 323 · see citing works

Feedback-regulated poly(ADP-ribosyl)ation by PARP-1 is required for rapid response to DNA damage in living cells

Mortusewicz, O., Amé, J., Schreiber, V., & Leonhardt, H. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm933 · Cited by 321 · see citing works

A CHO-cell strain having hypersensitivity to mutagens, a defect in DNA strand-break repair, and an extraordinary baseline frequency of sister-chromatid exchange

Thompson, L. H., Brookman, K. W., Dillehay, L. E., Carrano, A. V., Mazrimas, J. A., Mooney, C. L., & Minkler, J. L. (1982) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/0027-5107(82)90276-7 · Cited by 321 · see citing works

Macrodomain-containing proteins are new mono-ADP-ribosylhydrolases

Rosenthal, F., Feijs, K. L. H., Frugier, E., Bonalli, M., Forst, A. H., Imhof, R., Winkler, H. C., Fischer, D., Caflisch, A., Hassa, P. O., et al. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2521 · Cited by 317 · see citing works

Poly(ADP-Ribose) Polymerase 1 Accelerates Single-Strand Break Repair in Concert with Poly(ADP-Ribose) Glycohydrolase

Fisher, A. E. O., Hochegger, H., Takeda, S., & Caldecott, K. W. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.02248-06 · Cited by 315 · see citing works

Studies on the Polymer of Adenosine Diphosphate Ribose

Nishizuka, Y., Ueda, K., Nakazawa, K., & Hayaishi, O. (1967) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)95947-8 · Cited by 309 · see citing works

Deficiency of terminal ADP‐ribose protein glycohydrolase TARG1/C6orf130 in neurodegenerative disease

Sharifi, R., Morra, R., Appel, C. D., Tallis, M., Chioza, B. A., Jankevicius, G., Simpson, M. A., Matić, I., Sackey, E., Golia, B., et al. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.51 · Cited by 306 · see citing works

Spatial and Temporal Cellular Responses to Single-Strand Breaks in Human Cells

Okano, S., Lan, L., Caldecott, K. W., Mori, T., & Yasui, A. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.11.3974-3981.2003 · Cited by 305 · see citing works

Poly(ADP-ribose) Polymerase Null Mouse Cells Synthesize ADP-ribose Polymers

Shieh, W.-R., Amé, J., Wilson, M. V., Wang, Z., Koh, D. W., Jacobson, M. K., & Jacobson, E. L. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.46.30069 · Cited by 303 · see citing works

<i>In situ</i> analysis of repair processes for oxidative DNA damage in mammalian cells

Lan, L., Nakajima, S., Oohata, Y., Takao, M., Okano, S., Masutani, M., Wilson, S. H., & Yasui, A. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0406048101 · Cited by 299 · see citing works

Repair of and checkpoint response to topoisomerase I-mediated DNA damage

Pommier, Y. G., Redon, C., Rao, V. A., Seiler, J. A., Sordet, O., Takemura, H., Antony, S., Meng, L., Liao, Z., Kohlhagen, G., et al. (2003) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2003.08.016 · Cited by 299 · see citing works

Spatial and Temporal Cellular Responses to Single-Strand Breaks in Human Cells

Okano, S., Lan, L., Caldecott, K. W., Mori, T., & Yasui, A. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.15.5472.2003 · Cited by 297 · see citing works

Poly (ADP-ribose) polymerase (PARP) is not involved in base excision repair but PARP inhibition traps a single-strand intermediate

Ström, C. E., Johansson, F., Uhlén, M., Szigyarto, C. A., Erixon, K., & Helleday, T. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq1241 · Cited by 297 · see citing works

Characterization of the XRCC1-DNA ligase III complex in vitro and its absence from mutant hamster cells

Caldecott, K. W., Tucker, J. D., Lh, S., & Thompson, L. H. (1995) · Nucleic Acids Research · doi:10.1093/nar/23.23.4836 · Cited by 291 · see citing works

Mutations in PNKP cause microcephaly, seizures and defects in DNA repair

Shen, J., Gilmore, E. C., Marshall-Walker, C. A., Haddadin, M. H., Reynolds, J. J., Eyaid, W., Bodell, A., Barry, B. J., Gleason, D., Allen, K., et al. (2010) · Nature Genetics · doi:10.1038/ng.526 · Cited by 290 · see citing works

Generation of single-nucleotide repair patches following excision of uracil residues from DNA.

Dianov, G. L., Price, A., & Lindahl, T. L. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.4.1605 · Cited by 287 · see citing works

A screening method for isolating DNA repair-deficient mutants of CHO cells

Thompson, L. H., Rubin, J. S., Cleaver, J. E., Whitmore, G. F., & Brookman, K. W. (1980) · Somatic Cell and Molecular Genetics · doi:10.1007/bf01542791 · Cited by 282 · see citing works

Translesion DNA Synthesis and Mutagenesis in Eukaryotes

Sale, J. E. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a012708 · Cited by 282 · see citing works

The second zinc-finger domain of poly(ADP-ribose) polymerase determines specificity for single-stranded breaks in DNA.

Gradwohl, G., Murcia, J. M., Molinete, M., Simonin, F., Koken, M. H. M., Hoeijmakers, J. H. J., & de MURCIA, G. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.8.2990 · Cited by 277 · see citing works

Base Excision Repair and Lesion-Dependent Subpathways for Repair of Oxidative DNA Damage

Svilar, D., Goellner, E. M., Almeida, K. H., & Sobol, R. W. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3466 · Cited by 277 · 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

Proliferating cell nuclear antigen-dependent abasic site repair in Xenopus laevis oocytes: an alternative pathway of base excision DNA repair.

Matsumoto, Y., Kim, K., & Bogenhagen, D. F. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.9.6187 · Cited by 267 · see citing works

XRCC1 Protein Interacts with One of Two Distinct Forms of DNA Ligase III

Nash, R. A., Caldecott, K. W., Barnes, D. E., & Lindahl, T. L. (1997) · Biochemistry · doi:10.1021/bi962281m · Cited by 266 · 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

Structure of an XRCC1 BRCT domain: a new protein–protein interaction module

Zhang, X., Moréra, S., Bates, P. A., Whitehead, P. C., Coffer, A. I., Hainbucher, K., Nash, R. A., Sternberg, M. J. E., Lindahl, T. L., & Freemont, P. S. (1998) · The EMBO Journal · doi:10.1093/emboj/17.21.6404 · Cited by 252 · see citing works

Biologically Relevant Chemical Reactions of N7-Alkylguanine Residues in DNA

Gates, K. S., Nooner, T., & Dutta, S. (2004) · Chemical Research in Toxicology · doi:10.1021/tx049965c · Cited by 251 · see citing works

Human AP endonuclease 1 (APE1): From mechanistic insights to druggable target in cancer

Abbotts, R., & Madhusudan, S. (2010) · Cancer Treatment Reviews · doi:10.1016/j.ctrv.2009.12.006 · Cited by 250 · see citing works

Reconstitution of the DNA base excision—repair pathway

Dianov, G. L., & Lindahl, T. L. (1994) · Current Biology · doi:10.1016/s0960-9822(00)00245-1 · Cited by 250 · see citing works

Role of XRCC1 in the Coordination and Stimulation of Oxidative DNA Damage Repair Initiated by the DNA Glycosylase hOGG1

Marsin, S., Vidal, A. E., Sossou, M., Murcia, J. M., Page, F. L., Boiteux, S., de MURCIA, G., & Radicella, J. P. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306160200 · Cited by 244 · see citing works

The Human DNA Ligase III Gene Encodes Nuclear and Mitochondrial Proteins

Lakshmipathy, U., & Campbell, C. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.5.3869 · Cited by 243 · see citing works

Crystal Structures of Poly(ADP-ribose) Polymerase-1 (PARP-1) Zinc Fingers Bound to DNA

Langelier, M.-F., Planck, J. L., Roy, S., & Pascal, J. M. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.202507 · Cited by 239 · see citing works

The zinc fingers of human poly(ADP-ribose) polymerase are differentially required for the recognition of DNA breaks and nicks and the consequent enzyme activation. Other structures recognize intact DNA.

Ikejima, M., Noguchi, S., Yamashita, R., Ogura, T., Sügimura, T., Gill, D. M., & Miwa, M. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)45824-3 · Cited by 238 · see citing works

Physical and Functional Interaction between DNA Ligase IIIα and Poly(ADP-Ribose) Polymerase 1 in DNA Single-Strand Break Repair

Leppard, J. B., Dong, Z., Mackey, Z. B., & Tomkinson, A. E. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.16.5919-5927.2003 · Cited by 230 · see citing works

Poly(ADP-ribose) polymerase is a catalytic dimer and the automodification reaction is intermolecular.

Mendoza‐Alvarez, H., & Álvarez-González, R. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)41568-2 · Cited by 227 · see citing works

Crucial role for DNA ligase III in mitochondria but not in Xrcc1-dependent repair

Simsek, D., Furda, A. M., Gao, Y., Artus, J., Brunet, E., Hadjantonakis, A., Houten, B. V., Shuman, S., McKinnon, P. J., & Jasin, M. (2011) · Nature · doi:10.1038/nature09794 · Cited by 227 · see citing works

Poly (ADP-Ribose) synthetase. Separation and identification of three proteolytic fragments as the substrate-binding domain, the DNA-binding domain, and the automodification domain.

Kameshita, I., MATSUDA, Z., Taniguchi, T., & Shizuta, Y. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42913-9 · Cited by 225 · see citing works

PARP1–TDP1 coupling for the repair of topoisomerase I–induced DNA damage

Das, B. B., Huang, S.-Y. N., Murai, J., Rehman, I., Amé, J., Sengupta, S., Das, S., Majumdar, P., Zhang, H., Biard, D. S. F., et al. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku088 · Cited by 225 · see citing works

Poly(ADP-ribose) catabolism in mammalian cells exposed to DNA-damaging agents

Álvarez-González, R., & Althaus, F. R. (1989) · Mutation Research/DNA Repair · doi:10.1016/0921-8777(89)90012-8 · Cited by 224 · see citing works

U.v.-induced nuclear accumulation of p53 is evoked through DNA damage of actively transcribed genes independent of the cell cycle.

Yamaizumi, M., & Sugano, T. (1994) · PubMed · Cited by 224 · see citing works

Neonatal lethality with abnormal neurogenesis in mice deficient in DNA polymerase β

Sugo, N., Aratani, Y., Nagashima, Y., Kubota, Y., & Koyama, H. (2000) · The EMBO Journal · doi:10.1093/emboj/19.6.1397 · Cited by 221 · see citing works

ADP-ribosylation of histone H1. Identification of glutamic acid residues 2, 14, and the COOH-terminal lysine residue as modification sites.

Ogata, N., Ueda, K., Kagamiyama, H., & Hayaishi, O. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)43873-8 · Cited by 212 · see citing works

Purification and Properties of a Glycohydrolase from Calf Thymus Splitting Ribose-Ribose Linkages of Poly(Adenosine Diphosphate Ribose)

Miwa, M., Tanaka, M., Matsushima, T., & Sügimura, T. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)42597-0 · Cited by 209 · see citing works

A Third Zinc-binding Domain of Human Poly(ADP-ribose) Polymerase-1 Coordinates DNA-dependent Enzyme Activation

Langelier, M.-F., Servent, K. M., Rogers, E. E., & Pascal, J. M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m708558200 · Cited by 206 · see citing works

Effects of Uracil Incorporation, DNA Mismatches, and Abasic Sites on Cleavage and Religation Activities of Mammalian Topoisomerase I

Pourquier, P., Ueng, L.-M., Kohlhagen, G., Mazumder, A., Gupta, M., Kohn, K. W., & Pommier, Y. G. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.12.7792 · Cited by 204 · see citing works

A dominant-negative mutant of human poly(ADP-ribose) polymerase affects cell recovery, apoptosis, and sister chromatid exchange following DNA damage.

Schreiber, V., Hunting, D. J., Trucco, C., Gowans, B. J., Grünwald, D., de MURCIA, G., & Murcia, J. M. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.11.4753 · Cited by 203 · see citing works

The ataxia–oculomotor apraxia 1 gene product has a role distinct from ATM and interacts with the DNA strand break repair proteins XRCC1 and XRCC4

Clements, P. M., Breslin, C., Deeks, E. D., Byrd, P. J., Ju, L., Bieganowski, P., Brenner, C., Moreira, M.-C., Taylor, A. M. R., & Caldecott, K. W. (2004) · DNA repair · doi:10.1016/j.dnarep.2004.06.017 · Cited by 203 · see citing works

Genetic effects of thymine glycol: site-specific mutagenesis and molecular modeling studies.

Basu, A. K., Loechler, E. L., Leadon, S. A., & Essigmann, J. M. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.20.7677 · Cited by 202 · see citing works

XRCC1 is required for DNA single-strand break repair in human cells

Brem, R. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki543 · Cited by 201 · see citing works

XRCC1 co-localizes and physically interacts with PCNA

Fan, J. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh556 · Cited by 200 · see citing works

Association of XRCC1 and tyrosyl DNA phosphodiesterase (Tdp1) for the repair of topoisomerase I-mediated DNA lesions

Plo, I. (2003) · DNA repair · doi:10.1016/s1568-7864(03)00116-2 · Cited by 198 · see citing works

Repair of Formamidopyrimidines in DNA Involves Different Glycosylases

Hu, J., de Souza-Pinto, N. C., Haraguchi, K., Hogue, B. A., Jaruga, P., Greenberg, M. M., Dizdaroğlu, M., & Bohr, V. A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508772200 · Cited by 197 · see citing works

Tidying up loose ends: the role of polynucleotide kinase/phosphatase in DNA strand break repair

Weinfeld, M., Mani, R. S., Abdou, I., Aceytuno, R. D., & Glover, J. N. M. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2011.01.006 · Cited by 195 · see citing works

DNA ligase III is critical for mtDNA integrity but not Xrcc1-mediated nuclear DNA repair

Gao, Y., Katyal, S., Lee, Y., Zhao, J., Rehg, J. E., Russell, H. R., & McKinnon, P. J. (2011) · Nature · doi:10.1038/nature09773 · Cited by 193 · see citing works

Photoaffinity Labeling of Mouse Fibroblast Enzymes by a Base Excision Repair Intermediate

Lavrik, O. I., Prasad, R., Sobol, R. W., Horton, J. K., Ackerman, E. J., & Wilson, S. H. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102125200 · Cited by 189 · see citing works

Human DNA Polymerase β Deoxyribose Phosphate Lyase

Prasad, R., Beard, W. A., Strauss, P. R., & Wilson, S. H. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.24.15263 · Cited by 184 · see citing works

Solution structure of the single-strand break repair protein XRCC1 N-terminal domain.

Mullen, G. P., Marintchev, A., Mullen, M. A., Maciejewski, M. W., Pan, B., & Gryk, M. R. (1999) · Nature Structural Biology · doi:10.1038/12347 · Cited by 181 · see citing works

cDNA sequence, protein structure, and chromosomal location of the human gene for poly(ADP-ribose) polymerase.

Cherney, B., McBride, O. W., Chen, D. F., Alkhatib, H., Bhatia, K. G., Hensley, P., & Smulson, M. E. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.23.8370 · Cited by 181 · see citing works

A Shuttle Mechanism for DNA‐Protein Interactions

Zahradka, P. C., & Ebisuzaki, K. (1982) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1982.tb06912.x · Cited by 180 · see citing works

Interaction between ATM and PARP-1 in response to DNA damage and sensitization of ATM deficient cells through PARP inhibition

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

DNA single-strand break repair

Caldecott, K. W. (2014) · Experimental Cell Research · doi:10.1016/j.yexcr.2014.08.027 · Cited by 178 · see citing works

Role of poly(ADP-ribose) polymerase-1 in the removal of UV-induced DNA lesions by nucleotide excision repair

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

Aprataxin, a novel protein that protects against genotoxic stress

Gueven, N. (2004) · Human Molecular Genetics · doi:10.1093/hmg/ddh122 · Cited by 175 · see citing works

Genomic integrity and the ageing brain

Chow, H.-M., & Herrup, K. (2015) · Nature Reviews Neuroscience · doi:10.1038/nrn4020 · Cited by 174 · see citing works

The DNA-Binding Domain of Human PARP-1 Interacts with DNA Single-Strand Breaks as a Monomer through Its Second Zinc Finger

Eustermann, S., Videler, H., Yang, J., Cole, P. T., Gruszka, D. T., Veprintsev, D. B., & Neuhaus, D. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.01.034 · Cited by 174 · see citing works

Depletion of poly(ADP-ribose) polymerase by antisense RNA expression results in a delay in DNA strand break rejoining.

Ding, R., Pommier, Y. G., Kang, V., & Smulson, M. E. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42347-2 · Cited by 173 · see citing works

Histone shuttling by poly ADP-ribosylation

Althaus, F. R., Höfferer, L., Kleczkowska, H. E., Malanga, M., Naegeli, H., Panzeter, P. L., & Realini, C. A. (1994) · Springer eBooks · doi:10.1007/978-1-4615-2614-8_7 · Cited by 173 · see citing works

Homology and enzymatic requirements of microhomology-dependent alternative end joining

Sharma, S., Javadekar, S. M., Pandey, M., Srivastava, M., Kumari, R., & Raghavan, S. C. (2015) · Cell Death and Disease · doi:10.1038/cddis.2015.58 · Cited by 172 · see citing works

XRCC1 interactions with multiple DNA glycosylases: A model for its recruitment to base excision repair

Campalans, A., Marsin, S., Nakabeppu, Y., O'Connor, T. R., Boiteux, S., & Radicella, J. P. (2005) · DNA repair · doi:10.1016/j.dnarep.2005.04.014 · Cited by 170 · see citing works

Genetic diversity of UV-sensitive DNA repair mutants of Chinese hamster ovary cells.

Thompson, L. H., Busch, D. B., Brookman, K. W., Mooney, C. L., & Glaser, D. A. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.6.3734 · Cited by 169 · see citing works

Apurinic/apyrimidinic (AP) site recognition by the 5′-dRP/AP lyase in poly(ADP-ribose) polymerase-1 (PARP-1)

Khodyreva, S. N., Prasad, R., Ilina, E. S., Sukhanova, M. V., Kutuzov, M. M., Liu, Y., Hou, E. W., Wilson, S. H., & Lavrik, O. I. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1009182107 · Cited by 169 · see citing works

The Crystal Structure of Human Tyrosyl-DNA Phosphodiesterase, Tdp1

Davies, D. R., Interthal, H., Champoux, J. J., & Hol, W. G. J. (2002) · Structure · doi:10.1016/s0969-2126(02)00707-4 · Cited by 168 · see citing works

Toward specific functions of poly(ADP-ribose) polymerase-2

Yélamos, J., Schreiber, V., & Dantzer, F. (2008) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2008.02.003 · Cited by 167 · see citing works

The mechanism of the elongation and branching reaction of Poly(ADP-ribose) polymerase as derived from crystal structures and mutagenesis

Ruf, A., Rolli, V., de MURCIA, G., & Schulz, G. E. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.1673 · Cited by 166 · see citing works

Identification of the ADP-Ribosylation Sites in the PARP-1 Automodification Domain: Analysis and Implications

Tao, Z., Gao, P., & Liu, H. (2009) · Journal of the American Chemical Society · doi:10.1021/ja906135d · Cited by 166 · see citing works

CHIP-Mediated Degradation and DNA Damage-Dependent Stabilization Regulate Base Excision Repair Proteins

Parsons, J. L., Tait, P. S., Finch, D., Dianova, I. I., Allinson, S. L., & Dianov, G. L. (2008) · Molecular Cell · doi:10.1016/j.molcel.2007.12.027 · Cited by 165 · see citing works

The structural basis for the mutagenicity of O 6 -methyl-guanine lesions

Warren, J. J., Forsberg, L. J., & Beese, L. S. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0609580103 · Cited by 164 · see citing works

Processing of topoisomerase I cleavable complexes into DNA damage by transcription

Wu, J., & Liu, L. F. (1997) · Nucleic Acids Research · doi:10.1093/nar/25.21.4181 · Cited by 162 · see citing works

Histone shuttling by poly(ADP-ribosylation).

Realini, C. A., & Althaus, F. R. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)37040-1 · Cited by 162 · see citing works

APLF (C2orf13) Is a Novel Human Protein Involved in the Cellular Response to Chromosomal DNA Strand Breaks

Iles, N., Rulten, S. L., El‐Khamisy, S. F., & Caldecott, K. W. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.02269-06 · Cited by 159 · see citing works

PARP-1 and PARP-2: New players in tumour development.

Yélamos, J., Farrés, J., Llacuna, L., Ampurdanés, C., & Martín‐Caballero, J. (2011) · Europe PMC (PubMed Central) · Cited by 155 · see citing works

A novel human AP endonuclease with conserved zinc‐finger‐like motifs involved in DNA strand break responses

Kanno, S., Kuzuoka, H., Sasao, S., Hong, Z., Lan, L., Nakajima, S., & Yasui, A. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601663 · Cited by 153 · see citing works

Optimal function of the DNA repair enzyme TDP1 requires its phosphorylation by ATM and/or DNA‐PK

Das, B. B., Antony, S., Gupta, S., Dexheimer, T. S., Redon, C. E., Garfield, S., Shiloh, Y., & Pommier, Y. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.302 · Cited by 151 · see citing works

DNA Single-Strand Break Repair and Spinocerebellar Ataxia

Caldecott, K. W. (2003) · Cell · doi:10.1016/s0092-8674(02)01247-3 · Cited by 150 · see citing works

Poly(ADP-ribosylation) in vitro. Reaction parameters and enzyme mechanism.

Ferro, A. M., & Olivera, B. M. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)34453-3 · Cited by 149 · see citing works

Human Mre11/Human Rad50/Nbs1 and DNA Ligase IIIα/XRCC1 Protein Complexes Act Together in an Alternative Nonhomologous End Joining Pathway

Della-Maria, J., Zhou, Y., Tsai, M.-S., Kuhnlein, J., Carney, J. P., Paull, T. T., & Tomkinson, A. E. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.274159 · Cited by 148 · see citing works

Biologically relevant oxidants and terminology, classification and nomenclature of oxidatively generated damage to nucleobases and 2-deoxyribose in nucleic acids

Cadet, J., Loft, S. H., Oliński, R., Evans, M. D., Białkowski, K., Wagner, J. R., Dedon, P. C., Möller, P., Greenberg, M. M., & Cooke, M. S. (2012) · Free Radical Research · doi:10.3109/10715762.2012.659248 · Cited by 143 · see citing works

A New XRCC1-Containing Complex and Its Role in Cellular Survival of Methyl Methanesulfonate Treatment

Luo, H., Chan, D. W., Yang, T., Rodriguez, M. A., Chen, B. P.-C., Leng, M., Mu, J., Chen, D. J., Songyang, Z., Wáng, Y., et al. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.19.8356-8365.2004 · Cited by 142 · see citing works

Central Role for the Werner Syndrome Protein/Poly(ADP-Ribose) Polymerase 1 Complex in the Poly(ADP-Ribosyl)ation Pathway after DNA Damage

von Kobbe, C., Harrigan, J. A., May, A., Opresko, P. L., Dawut, L., Cheng, W., & Bohr, V. A. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.23.8601-8613.2003 · Cited by 140 · see citing works

Cytosine Methylation and DNA Repair

Walsh, C. P., & Xu, G. L. (2006) · Springer eBooks · doi:10.1007/3-540-31390-7_11 · Cited by 139 · see citing works

Poly ADP-ribosylation: a histone shuttle mechanism in DNA excision repair

Us, F. R. A. (1992) · Journal of Cell Science · doi:10.1242/jcs.102.4.663 · Cited by 139 · see citing works

XRCC1-DNA polymerase interaction is required for efficient base excision repair

Dianova, I. I. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh567 · Cited by 138 · see citing works

The role of DNA repair in brain related disease pathology

Canugovi, C., Misiak, M., Ferrarelli, L. K., Croteau, D. L., & Bohr, V. A. (2013) · DNA repair · doi:10.1016/j.dnarep.2013.04.010 · Cited by 136 · see citing works

DNA polymerase β deficiency leads to neurodegeneration and exacerbates Alzheimer disease phenotypes

Sýkora, P., Misiak, M., Wang, Y., Ghosh, S., Leandro, G. D. S., Liu, D., Tian, J. Y., Baptiste, B. A., Cong, W., Brenerman, B. M., et al. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku1356 · Cited by 136 · see citing works

Human base excision repair enzymes apurinic/apyrimidinic endonuclease1 (APE1), DNA polymerase and poly(ADP-ribose) polymerase 1: interplay between strand-displacement DNA synthesis and proofreading exonuclease activity

Sukhanova, M. V. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki266 · Cited by 135 · see citing works

Mutations in PNKP Cause Recessive Ataxia with Oculomotor Apraxia Type 4

Brás, J., Alonso, I. D. C. M. P., Barbot, C., Costa, M. M., Darwent, L., Orme, T., Sequeiros, J., Hardy, J., Coutinho, P., & Guerreiro, R. J. (2015) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2015.01.005 · Cited by 133 · see citing works

Base excision repair is efficient in cells lacking poly(ADP-ribose) polymerase 1

Vodenicharov, M. D. (2000) · Nucleic Acids Research · doi:10.1093/nar/28.20.3887 · Cited by 131 · see citing works

The response of Parp knockout mice against DNA damaging agents

Masutani, M., Nozaki, T., Nakamoto, K., Nakagama, H., Suzuki, H. I., Kusuoka, O., Tsutsumi, M., & Sugimura, T. (2000) · Mutation Research/Reviews in Mutation Research · doi:10.1016/s1383-5742(00)00033-8 · Cited by 130 · see citing works

Primary structure of human poly(ADP-ribose) synthetase as deduced from cDNA sequence.

Kurosaki, T., Ushiro, H., Mitsuuchi, Y., Suzuki, S., Matsuda, M., Matsuda, Y., Katunuma, N., Kangawa, K., Matsuo, H., & Hirose, T. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47687-9 · Cited by 129 · see citing works

A Cell Cycle-Specific Requirement for the XRCC1 BRCT II Domain during Mammalian DNA Strand Break Repair

Taylor, R., Moore, D. J., Whitehouse, J., Johnson, P., & Caldecott, K. W. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.2.735-740.2000 · Cited by 126 · see citing works

Large-scale isolation of UV-sensitive clones of CHO cells

Busch, D. B., Cleaver, J. E., & Glaser, D. A. (1980) · Somatic Cell and Molecular Genetics · doi:10.1007/bf01542792 · Cited by 123 · see citing works

An Alternative Splicing Event Which Occurs in Mouse Pachytene Spermatocytes Generates a Form of DNA Ligase III with Distinct Biochemical Properties That May Function in Meiotic Recombination

Mackey, Z. B., Ramos, W., Levin, D. S., Walter, C. A., McCarrey, J. R., & Tomkinson, A. E. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.2.989 · Cited by 123 · see citing works

Domain specific interaction in the XRCC1-DNA polymerase beta complex

Marintchev, A. (2000) · Nucleic Acids Research · doi:10.1093/nar/28.10.2049 · Cited by 118 · see citing works

Poly(ADP-ribose) Polymerase 1 (PARP-1) Binds to 8-Oxoguanine-DNA Glycosylase (OGG1)

Hooten, N. N., Kompaniez, K., Barnes, J., Lohani, A., & Evans, M. K. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.255869 · Cited by 116 · see citing works

Single molecule detection of PARP1 and PARP2 interaction with DNA strand breaks and their poly(ADP-ribosyl)ation using high-resolution AFM imaging

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

DNA damage control: regulation and functions of checkpoint kinase 1

Smits, V. A. J., & Gillespie, D. A. (2015) · FEBS Journal · doi:10.1111/febs.13387 · Cited by 115 · see citing works

RPA and ATR link transcriptional stress to p53

Derheimer, F. A., O’Hagan, H. M., Krueger, H., Hanasoge, S., Paulsen, M. T., & Ljungman, M. E. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0705317104 · Cited by 114 · see citing works

The genesis of cerebellar interneurons and the prevention of neural DNA damage require XRCC1

Lee, Y., Katyal, S., Li, Y., El‐Khamisy, S. F., Russell, H. R., Caldecott, K. W., & McKinnon, P. J. (2009) · Nature Neuroscience · doi:10.1038/nn.2375 · Cited by 114 · see citing works

ADP-ribosylhydrolase 3 (ARH3), Not Poly(ADP-ribose) Glycohydrolase (PARG) Isoforms, Is Responsible for Degradation of Mitochondrial Matrix-associated Poly(ADP-ribose)

Niere, M., Mashimo, M., Agledal, L., Dölle, C., Kasamatsu, A., Kato, J., Moss, J., & Ziegler, M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.349183 · Cited by 113 · see citing works

Purification and properties of poly(adenosine diphosphate ribose) synthetase.

Okayama, H., Edson, C. M., Fukushima, M., Ueda, K., & Hayaishi, O. (1977) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)66926-7 · Cited by 111 · see citing works

HSP90 regulates DNA repair via the interaction between XRCC1 and DNA polymerase β

Fang, Q., Inanç, B., Schamus, S., Wang, X., Wei, L., Brown, A. R., Svilar, D., Sugrue, K. F., Goellner, E. M., Zeng, X., et al. (2014) · Nature Communications · doi:10.1038/ncomms6513 · Cited by 111 · see citing works

Interactive effects of inhibitors of poly(ADP-ribose) polymerase and DNA-dependent protein kinase on cellular responses to DNA damage

Boulton, S. J. (1999) · Carcinogenesis · doi:10.1093/carcin/20.2.199 · Cited by 111 · see citing works

The XRCC1 phosphate-binding pocket binds poly (ADP-ribose) and is required for XRCC1 function

Breslin, C., Hornyák, P., Ridley, A. J., Rulten, S. L., Hanzlíková, H., Oliver, A. W., & Caldecott, K. W. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv623 · Cited by 107 · see citing works

APOBEC3B can impair genomic stability by inducing base substitutions in genomic DNA in human cells

Shinohara, M., Io, K., Shindo, K., Matsui, M., Sakamoto, T., Tada, K., Kobayashi, M., Kadowaki, N., & Takaori‐Kondo, A. (2012) · Scientific Reports · doi:10.1038/srep00806 · Cited by 102 · see citing works

APLF (C2orf13) facilitates nonhomologous end-joining and undergoes ATM-dependent hyperphosphorylation following ionizing radiation

Macrae, C. J., McCulloch, R. D., Ylanko, J., Durocher, D., & Koch, C. A. (2008) · DNA repair · doi:10.1016/j.dnarep.2007.10.008 · Cited by 102 · see citing works

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 · see citing works

DNA damage repair: historical perspectives, mechanistic pathways and clinical translation for targeted cancer therapy

Huang, R., & Zhou, P. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00648-7 · Cited by 948 · see citing works

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 865 · see citing works

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 719 · see citing works

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 · see citing works

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 382 · see citing works

Oxidative DNA damage & repair: An introduction

Cadet, J., & Davies, K. J. A. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.03.030 · Cited by 339 · see citing works

Carcinogens and DNA damage

Barnes, J. L., Zubair, M., John, K., Poirier, M. C., & Martin, F. L. (2018) · Biochemical Society Transactions · doi:10.1042/bst20180519 · Cited by 320 · see citing works

Sperm DNA Fragmentation: A New Guideline for Clinicians

Agarwal, A. K., Majzoub, A. A., Baskaran, S., Selvam, M. K. P., Cho, C., Henkel, R., Finelli, R., Leisegang, K., Sengupta, P., Zenoaga-Barbăroşie, C., et al. (2020) · The World Journal of Men s Health · doi:10.5534/wjmh.200128 · Cited by 341 · see citing works

ATM in DNA repair in cancer

Jin, M. H., & Oh, D. (2019) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2019.07.002 · Cited by 246 · see citing works

DNA Damage: From Threat to Treatment

Carusillo, A., & Mussolino, C. (2020) · Cells · doi:10.3390/cells9071665 · Cited by 246 · see citing works

DNA Damage and Associated DNA Repair Defects in Disease and Premature Aging

Tiwari, V., & Wilson, D. M. (2019) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2019.06.005 · Cited by 244 · 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

Comet assay: a versatile but complex tool in genotoxicity testing

Cordelli, E., Bignami, M., & Pacchierotti, F. (2021) · Toxicology Research · doi:10.1093/toxres/tfaa093 · Cited by 189 · see citing works

Genome integrity and disease prevention in the nervous systemPreprint

McKinnon, P. J. (2017) · Genes & Development · doi:10.1101/gad.301325.117 · Cited by 155 · see citing works

Roles of UVA radiation and DNA damage responses in melanoma pathogenesis

Khan, A. Q., Travers, J. B., & Kemp, M. G. (2018) · Environmental and Molecular Mutagenesis · doi:10.1002/em.22176 · Cited by 152 · see citing works

Dancing with the DNA damage response: next-generation anti-cancer therapeutic strategies

Minchom, A. R., Aversa, C., & Lopez, J. S. (2018) · Therapeutic Advances in Medical Oncology · doi:10.1177/1758835918786658 · Cited by 138 · see citing works

Causes and consequences of DNA single-strand breaks

Caldecott, K. W. (2023) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2023.11.001 · Cited by 132 · see citing works

Redox dysregulation as a driver for DNA damage and its relationship to neurodegenerative diseases

Shadfar, S., Parakh, S., Jamali, M. S., & Atkin, J. D. (2023) · Translational Neurodegeneration · doi:10.1186/s40035-023-00350-4 · Cited by 135 · see citing works

Base Excision Repair: Mechanisms and Impact in Biology, Disease, and Medicine

Gohil, D., Sarker, A. H., & Roy, R. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241814186 · Cited by 136 · see citing works

Role of Rad51 and DNA repair in cancer: A molecular perspective

Laurini, E., Marson, D., Fermeglia, A., Aulić, S., Fermeglia, M., & Pricl, S. (2020) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2020.107492 · Cited by 128 · see citing works

Genome-wide Nucleotide-Resolution Mapping of DNA Replication Patterns, Single-Strand Breaks, and Lesions by GLOE-Seq

Sriramachandran, A. M., Petrosino, G., Méndez-Lago, M., Schäfer, A. J., Batista-Nascimento, L. S., Zilio, N., & Ulrich, H. D. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.03.027 · Cited by 111 · see citing works

BRCA Mutations in Prostate Cancer: Assessment, Implications and Treatment Considerations

Shah, S., Rachmat, R., Enyioma, S., Ghose, A., Revythis, A., & Boussios, S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222312628 · Cited by 107 · see citing works

Targeting PARP proteins in acute leukemia: DNA damage response inhibition and therapeutic strategies

Padella, A., di Rorà, A. G. L., Marconi, G., Ghetti, M., Martinelli, G., & Simonetti, G. (2022) · Journal of Hematology & Oncology · doi:10.1186/s13045-022-01228-0 · Cited by 102 · see citing works

Antimicrobial carbon materials-based quantum dots: From synthesis strategies to antibacterial properties for diagnostic and therapeutic applications in wound healing

Zare, I., Nasab, S. Z., Rahi, A., Ghaee, A., Koohkhezri, M., Farani, M. R., Gholipour, H. M., Atabaki, A. H., Hamblin, M. R., Mostafavi, E., et al. (2024) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2024.216211 · Cited by 96 · see citing works

OGG1-initiated base excision repair exacerbates oxidative stress-induced parthanatos

Wang, R., Li, C., Qiao, P., Xue, Y., Zheng, X., Chen, H., Zeng, X., Liu, W., Boldogh, I. R., & Ba, X. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-0680-0 · Cited by 94 · see citing works

IGFBP-3 interacts with NONO and SFPQ in PARP-dependent DNA damage repair in triple-negative breast cancer

de Silva, H. C., Lin, M. Z., Phillips, L., Martin, J. L., & Baxter, R. C. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03033-4 · Cited by 84 · see citing works

Discovery of the Involvement in DNA Oxidative Damage of Human Sperm Nuclear Basic Proteins of Healthy Young Men Living in Polluted Areas

Lettieri, G., D’Agostino, G., Mele, E., Cardito, C., Esposito, R., Cimmino, A., Giarra, A., Trifuoggi, M., Raimondo, S., Notari, T., et al. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21124198 · Cited by 84 · see citing works

The Effects of Ionising and Non-Ionising Electromagnetic Radiation on Extracellular Matrix Proteins

Tuieng, R. J., Cartmell, S. H., Kirwan, C., & Sherratt, M. J. (2021) · Cells · doi:10.3390/cells10113041 · Cited by 85 · see citing works

Medicinal Thiols: Current Status and New Perspectives

Pfaff, A. R., Beltz, J., King, E., & Nuran Ercal, A. (2019) · Mini-Reviews in Medicinal Chemistry · doi:10.2174/1389557519666191119144100 · Cited by 82 · see citing works

Targeting DNA Damage Response in Prostate and Breast Cancer

Wengner, A. M., Scholz, A., & Haendler, B. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21218273 · Cited by 78 · see citing works

Key biological mechanisms involved in high-LET radiation therapies with a focus on DNA damage and repair

Nikitaki, Z., Velalopoulou, A. P., Zanni, V., Tremi, I., Havaki, S., Kokkoris, M., Gorgoulis, V. G., Koumenis, C., & Georgakilas, A. G. (2022) · Expert Reviews in Molecular Medicine · doi:10.1017/erm.2022.6 · Cited by 80 · see citing works

Single-Strand Break End Resection in Genome Integrity: Mechanism and Regulation by APE2

Hossain, M. A., Lin, Y., & Yan, S. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19082389 · Cited by 74 · see citing works

Synergistic lethality between PARP-trapping and alantolactone-induced oxidative DNA damage in homologous recombination-proficient cancer cells

Wang, H., Shan, Z., Song, L., Qu, M., & Zou, Z. (2020) · Oncogene · doi:10.1038/s41388-020-1191-x · Cited by 69 · see citing works

Multilevel Mechanisms of Cancer Drug Resistance

Roszkowska, M. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252212402 · Cited by 73 · see citing works

Temporal dynamics of base excision/single-strand break repair protein complex assembly/disassembly are modulated by the PARP/NAD+/SIRT6 axis

Koczor, C. A., Saville, K. M., Andrews, J., Clark, J., Fang, Q., Li, J., Al‐Rahahleh, R. Q., Ibrahim, M., McClellan, S. B., Makarov, M. V., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109917 · Cited by 66 · see citing works

The contribution of PARP1, PARP2 and poly(ADP-ribosyl)ation to base excision repair in the nucleosomal context

Kutuzov, M. M., Belousova, E. A., Kurgina, T. A., Ukraintsev, A. A., Васильева, И. А., Khodyreva, S. N., & Lavrik, O. I. (2021) · Scientific Reports · doi:10.1038/s41598-021-84351-1 · Cited by 64 · see citing works

DNA folds threaten genetic stability and can be leveraged for chemotherapy

Zell, J., Sperti, F. R., Britton, S., & Monchaud, D. (2020) · RSC Chemical Biology · doi:10.1039/d0cb00151a · Cited by 58 · see citing works

DNA Damage Response in Prostate CancerPreprint

Schiewer, M. J., & Knudsen, K. E. (2018) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a030486 · Cited by 58 · see citing works

The base excision repair process: comparison between higher and lower eukaryotes

Hindi, N. N., Elsakrmy, N., & Ramotar, D. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-03990-9 · Cited by 55 · see citing works

ALC1/CHD1L, a chromatin-remodeling enzyme, is required for efficient base excision repair

Tsuda, M., Cho, K., Ooka, M., Shimizu, N., Watanabe, R., Yasui, A., Nakazawa, Y., Ogi, T., Harada, H., Agama, K., et al. (2017) · PLoS ONE · doi:10.1371/journal.pone.0188320 · Cited by 51 · see citing works

Genome-wide analysis of 8-oxo-7,8-dihydro-2'-deoxyguanosine at single-nucleotide resolution unveils reduced occurrence of oxidative damage at G-quadruplex sites

An, J., Yin, M., Yin, J., Wu, S., Selby, C. P., Yang, Y., Sancar, A., Xu, G.-L., Qian, M., & Hu, J. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab1022 · Cited by 49 · see citing works

PARP inhibitors alone and in combination with other biological agents in homologous recombination deficient epithelial ovarian cancer: From the basic research to the clinic

Gadducci, A., & Guerrieri, M. E. (2017) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2017.04.006 · Cited by 49 · see citing works

Role of condensates in modulating DNA repair pathways and its implication for chemoresistance

Dall’Agnese, G., Dall’Agnese, A., Banani, S. F., Codrich, M., Malfatti, M. C., Antoniali, G., & Tell, G. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.104800 · Cited by 47 · see citing works

The cerebellar degeneration in ataxia-telangiectasia: A case for genome instability

Shiloh, Y. (2020) · DNA repair · doi:10.1016/j.dnarep.2020.102950 · Cited by 47 · see citing works

Molecular effects of polystyrene nanoplastics on human neural stem cells

Martín-Folgar, R., González, M. D. C., Torres-Ruíz, M., Cañas, A., de Alba-Gonzalez, M., Liste, I., & Morales, M. (2024) · PLoS ONE · doi:10.1371/journal.pone.0295816 · Cited by 45 · see citing works

Protein–Protein Interactions in DNA Base Excision Repair

Moor, N. A., & Lavrik, O. I. (2018) · Biochemistry (Moscow) · doi:10.1134/s0006297918040120 · Cited by 45 · see citing works

Formation and Repair of an Interstrand DNA Cross-Link Arising from a Common Endogenous Lesion

Housh, K., Jha, J. S., Yang, Z., Haldar, T., Johnson, K. M., Yin, J., Wang, Y., & Gates, K. S. (2021) · Journal of the American Chemical Society · doi:10.1021/jacs.1c06926 · Cited by 43 · see citing works

The potential of PARP inhibitors in targeted cancer therapy and immunotherapy

Hunia, J., Gawalski, K., Szredzka, A., Suskiewicz, M. J., & Nowis, D. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.1073797 · Cited by 45 · see citing works

PARP1 condensates differentially partition DNA repair proteins and enhance DNA ligation

Sang, C. C., Moore, G., Tereshchenko, M., Zhang, H., Nosella, M. L., Dasovich, M., Alderson, T. R., Leung, A. K. L., Finkelstein, I. J., Forman-Kay, J. D., et al. (2024) · EMBO Reports · doi:10.1038/s44319-024-00285-5 · Cited by 40 · see citing works

PCNA cycling dynamics during DNA replication and repair in mammals

Kang, S., Yoo, J., & Myung, K. (2024) · Trends in Genetics · doi:10.1016/j.tig.2024.02.006 · Cited by 38 · see citing works

Minireview Exploring the Biological Cycle of Vitamin B3 and Its Influence on Oxidative Stress: Further Molecular and Clinical Aspects

Doroftei, B., Ilie, O., Cojocariu, R.-O., Ciobica, A. S., Maftei, R., Grab, D., Anton, E., McKenna, J., Dhunna, N., & Simionescu, G. (2020) · Molecules · doi:10.3390/molecules25153323 · Cited by 38 · see citing works

An Emerging Regulatory Role for the Tumor Microenvironment in the DNA Damage Response to Double-Strand Breaks

Lama-Sherpa, T. D., & Shevde, L. A. (2019) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-19-0665 · Cited by 36 · see citing works

Signaling pathways involved in cell cycle arrest during the DNA breaks

Sadoughi, F., Hallajzadeh, J., Asemi, Z., Mansournia, M. A., Alemi, F., & Yousefi, B. (2021) · DNA repair · doi:10.1016/j.dnarep.2021.103047 · Cited by 39 · see citing works

The relationship between DNA single-stranded damage response and double-stranded damage response

Ma, A., & Dai, X. (2017) · Cell Cycle · doi:10.1080/15384101.2017.1403681 · Cited by 38 · see citing works

Topoisomerase I-driven repair of UV-induced damage in NER-deficient cells

Saha, L. K., Wakasugi, M., Akter, S., Prasad, R., Wilson, S. H., Shimizu, N., Sasanuma, H., Huang, S.-Y. N., Agama, K., Pommier, Y. G., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1920165117 · Cited by 36 · see citing works

Toxicity and chemical transformation of silver nanoparticles in A549 lung cells: dose-rate-dependent genotoxic impact

Bobyk, L., Tarantini, A., Beal, D. M., Veronesi, G., Kieffer, I., Motellier, S., Valsami‐Jones, E., Lynch, I., Jouneau, P., Pernet‐Gallay, K., et al. (2021) · Environmental Science Nano · doi:10.1039/d0en00533a · Cited by 35 · see citing works

Effector memory T cells induce innate inflammation by triggering DNA damage and a non-canonical STING pathway in dendritic cells

Meibers, H. E., Warrick, K. A., VonHandorf, A., Vallez, C. N., Kawarizadeh, K., Saha, I., Donmez, O. A., Jain, V. G., Kottyan, L. C., Weirauch, M. T., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.113180 · Cited by 34 · see citing works

The future of cancer treatment: combining radiotherapy with immunotherapy

Dagar, G., Gupta, A., Shankar, A., Chauhan, R., Macha, M. A., Bhat, A. A., Das, D., Goyal, R., Bhoriwal, S. K., PANDITA, R. K., et al. (2024) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2024.1409300 · Cited by 34 · see citing works

Molecular Mechanisms Regulating the DNA Repair Protein APE1: A Focus on Its Flexible N-Terminal Tail Domain

López, D. J., Rodríguez, J. A., & Bañuelos, S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22126308 · Cited by 34 · see citing works

Dynamic light scattering study of base excision DNA repair proteins and their complexes

Васильева, И. А., Anarbaev, R. O., Moor, N. A., & Lavrik, O. I. (2018) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2018.10.009 · Cited by 33 · see citing works

DNA damage signaling in the cellular responses to mustard vesicants

Jan, Y.-H., Heck, D. E., Laskin, D. L., & Laskin, J. D. (2020) · Toxicology Letters · doi:10.1016/j.toxlet.2020.03.008 · Cited by 32 · see citing works

DNA2—An Important Player in DNA Damage Response or Just Another DNA Maintenance Protein?

Pawłowska, E., Szczepańska, J., & Błasiak, J. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18071562 · Cited by 32 · see citing works

The CHK1 inhibitor SRA737 synergizes with PARP1 inhibitors to kill carcinoma cells

Booth, L. A., Roberts, J. L., Poklepovic, A. S., & Dent, P. (2018) · Cancer Biology & Therapy · doi:10.1080/15384047.2018.1472189 · Cited by 31 · see citing works

DNA Damage Response in Multiple Myeloma: The Role of the Tumor Microenvironment

Saitoh, T., & Oda, T. (2021) · Cancers · doi:10.3390/cancers13030504 · Cited by 31 · see citing works

Functional Roles of PARP2 in Assembling Protein–Protein Complexes Involved in Base Excision DNA Repair

Васильева, И. А., Moor, N. A., Anarbaev, R. O., Kutuzov, M. M., & Lavrik, O. I. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094679 · Cited by 31 · see citing works

BCL2-overexpressing prostate cancer cells rely on PARP1-dependent end-joining and are sensitive to combined PARP inhibitor and radiation therapy

Oing, C., Tennstedt, P., Simon, R., Volquardsen, J., Borgmann, K., Bokemeyer, C., Petersen, C., Dikomey, E., Rothkamm, K., & Mansour, W. Y. (2018) · Cancer Letters · doi:10.1016/j.canlet.2018.03.007 · Cited by 31 · see citing works

Apurinic endonuclease-1 preserves neural genome integrity to maintain homeostasis and thermoregulation and prevent brain tumors

Dumitrache, L. C., Shimada, M., Downing, S. M., Kwak, Y. D., Li, Y., Illuzzi, J. L., Russell, H. R., Wilson, D. M., & McKinnon, P. J. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1809682115 · Cited by 31 · see citing works

The scaffold protein XRCC1 stabilizes the formation of polβ/gap DNA and ligase IIIα/nick DNA complexes in base excision repair

Tang, Q., & Çağlayan, M. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.101025 · Cited by 30 · see citing works

Oxidative DNA Damage in the Pathophysiology of Spinal Cord Injury: Seems Obvious, but Where Is the Evidence?

Scheijen, E. E. M., Hendrix, S., & Wilson, D. M. (2022) · Antioxidants · doi:10.3390/antiox11091728 · Cited by 30 · see citing works

Single-stranded DNA damage: Protecting the single-stranded DNA from chemical attack

Anindya, R. (2020) · DNA repair · doi:10.1016/j.dnarep.2020.102804 · Cited by 30 · see citing works

Genomic alterations and abnormal expression of APE2 in multiple cancers

Jensen, K. A., Shi, X. M., & Yan, S. (2020) · Scientific Reports · doi:10.1038/s41598-020-60656-5 · Cited by 30 · see citing works

DNA damage in cancer development: special implications in viral oncogenesis.

Katerji, M., & Duerksen-Hughes, P. J. (2021) · PubMed Central · Cited by 29 · see citing works

Timely termination of repair DNA synthesis by ATAD5 is important in oxidative DNA damage-induced single-strand break repair

Park, S. H., Kim, Y., Ra, J. S., Wie, M., Kang, M.-S., Kang, S., Myung, K., & Lee, K. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab999 · Cited by 27 · see citing works

Human apurinic/apyrimidinic endonuclease 1 is modified in vitro by poly(ADP-ribose) polymerase 1 under control of the structure of damaged DNA

Moor, N. A., Васильева, И. А., Kuznetsov, N. A., & Lavrik, O. I. (2019) · Biochimie · doi:10.1016/j.biochi.2019.10.011 · Cited by 29 · see citing works

Nuclear myosins – roles for molecular transporters and anchors

Cook, A. W., Gough, R. E., & Toseland, C. P. (2020) · Journal of Cell Science · doi:10.1242/jcs.242420 · Cited by 28 · see citing works

A non‐proteolytic release mechanism for HMCES‐DNA‐protein crosslinks

Donsbach, M., Dürauer, S., Grünert, F., Nguyen, K. T., Nigam, R., Yaneva, D., Weickert, P., Bezalel‐Buch, R., Semlow, D. R., & Stingele, J. (2023) · The EMBO Journal · doi:10.15252/embj.2022113360 · Cited by 27 · see citing works

Enzyme-Activated Generation of Reactive Oxygen Species from Heterocyclic N-Oxides under Aerobic and Anaerobic Conditions and Its Relevance to Hypoxia-Selective Prodrugs

Shen, X., & Gates, K. S. (2019) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.9b00036 · Cited by 27 · see citing works

Alkannin-Induced Oxidative DNA Damage Synergizes With PARP Inhibition to Cause Cancer-Specific Cytotoxicity

Ming-xin, C., Wang, H., Niu, J., Song, Y., & Zou, Z. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.610205 · Cited by 26 · see citing works

Reconsidering the Chemical Nature of Strand Breaks Derived from Abasic Sites in Cellular DNA: Evidence for 3′-Glutathionylation

Jha, J. S., Yin, J., Haldar, T., Yang, Z., Wang, Y., & Gates, K. S. (2022) · Journal of the American Chemical Society · doi:10.1021/jacs.2c02703 · Cited by 25 · see citing works

The Relationship Between Single-Nucleotide Polymorphisms, the Expression of DNA Damage Response Genes, and Hepatocellular Carcinoma in a Polish Population

Krupa, R., Czarny, P. L., Wigner, P., Woźny, J., Jabłkowski, M., Kordek, R., Szemraj, J., & Śliwiński, T. (2017) · DNA and Cell Biology · doi:10.1089/dna.2017.3664 · Cited by 26 · see citing works

Genome Integrity and Neurological Disease

Scheijen, E. E. M., & Wilson, D. M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23084142 · Cited by 24 · see citing works

Oxidatively generated tandem DNA modifications by pyrimidinyl and 2-deoxyribosyl peroxyl radicals

Robert, G., Wagner, J. R., & Cadet, J. (2023) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2022.12.104 · Cited by 24 · see citing works

E3 ligases: a ubiquitous link between DNA repair, DNA replication and human disease

Chauhan, A. S., Jhujh, S. S., & Stewart, G. S. (2024) · Biochemical Journal · doi:10.1042/bcj20240124 · Cited by 21 · see citing works

Persistent pesticides: effects of endosulfan at the molecular level on the aquatic invertebrate Chironomus riparius

Muñiz‐González, A., Novo, M., & Martínez‐Guitarte, J. (2021) · Environmental Science and Pollution Research · doi:10.1007/s11356-021-12669-4 · Cited by 23 · see citing works

Repurposing Ceritinib Induces DNA Damage and Enhances PARP Inhibitor Responses in High-Grade Serous Ovarian Carcinoma

Kanakkanthara, A., Hou, X., Ekstrom, T. L., Zanfagnin, V., Huehls, A. M., Kelly, R. L., Ding, H., Larson, M. C., Vasmatzis, G., Oberg, A. L., et al. (2021) · Cancer Research · doi:10.1158/0008-5472.can-21-0732 · Cited by 23 · see citing works

Synthesis and biological evaluation of a tumor-selective degrader of PARP1

Pu, C., Wang, S., Luo, D., Liu, Y., Ma, X., Zhang, H., Yu, S., Lan, S., Huang, Q., Deng, R., et al. (2022) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2022.116908 · Cited by 23 · see citing works

Cas9/Nickase-induced allelic conversion by homologous chromosome-templated repair in Drosophila somatic cells

Roy, S., Juste, S. S., Sneider, M., Auradkar, A., Klanseck, C. F., Li, Z., Julio, A. H. F., Amo, V. L. D., Bier, E., & Guichard, A. (2022) · Science Advances · doi:10.1126/sciadv.abo0721 · Cited by 23 · see citing works

Modulation of DNA Damage Response by Sphingolipid Signaling: An Interplay that Shapes Cell Fate

Francis, M., Daher, A. A., Azzam, P., Mroueh, M., & Zeidan, Y. H. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21124481 · Cited by 22 · see citing works

Polymerases and DNA Repair in Neurons: Implications in Neuronal Survival and Neurodegenerative Diseases

Li, X., Cao, G., Liu, X., Tang, T.-S., Guo, C., & Liu, H. (2022) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2022.852002 · Cited by 22 · see citing works

Plant DNA Repair Pathways and Their Applications in Genome Engineering

Que, Q., Chen, Y., Kelliher, T., Skibbe, D. S., Dong, S., & Chilton, M.-D. (2019) · Methods in molecular biology · doi:10.1007/978-1-4939-8991-1_1 · Cited by 21 · see citing works

Impact of PARP1, PARP2 & PARP3 on the Base Excision Repair of Nucleosomal DNA

Kutuzov, M. M., Belousova, E. A., Ilina, E. S., & Lavrik, O. I. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-41283-8_4 · Cited by 20 · see citing works

Role of phase partitioning in coordinating DNA damage response: focus on the Apurinic Apyrimidinic Endonuclease 1 interactome

Tosolini, D., Antoniali, G., Dalla, E., & Tell, G. (2020) · BioMolecular Concepts · doi:10.1515/bmc-2020-0019 · Cited by 20 · see citing works

Association of Caspase 3 Activation and H2AX γ Phosphorylation in the Aging Brain: Studies on Untreated and Irradiated Mice

Gionchiglia, N., Granato, A., Merighi, A., & Lossi, L. (2021) · Biomedicines · doi:10.3390/biomedicines9091166 · Cited by 19 · see citing works

New Methodologies to Study DNA Repair Processes in Space and Time Within Living Cells

Zentout, S., Smith, R., Jacquier, M., & Huet, S. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.730998 · Cited by 20 · see citing works

Role of Antioxidants of Natural Herbs in Management of Male Infertility

Gaznee, Kohli, A., & Kumar, R. (2023) · Journal for Research in Applied Sciences and Biotechnology · doi:10.55544/jrasb.2.1.9 · Cited by 19 · see citing works

Targeting DNA Damage Repair and Immune Checkpoint Proteins for Optimizing the Treatment of Endometrial Cancer

Bian, X., Sun, C., Cheng, J., & Hong, B. (2023) · Pharmaceutics · doi:10.3390/pharmaceutics15092241 · Cited by 19 · see citing works

Poly(ADP-ribose) polymerase 1 (PARP1) promotes oxidative stress–induced association of Cockayne syndrome group B protein with chromatin

Boetefuer, E. L., Lake, R. J., Dreval, K., & Fan, H.-Y. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.004548 · Cited by 19 · see citing works

Bcl2-Expressing Quiescent Type B Neural Stem Cells in the Ventricular–Subventricular Zone Are Resistant to Concurrent Temozolomide/X-Irradiation

Cameron, B. D., Traver, G. L., Roland, J. T., Brockman, A. A., Dean, D., Johnson, L. S., Boyd, K. L., Ihrie, R. A., & Freeman, M. L. (2019) · Stem Cells · doi:10.1002/stem.3081 · Cited by 19 · see citing works

Functional Role of N-Terminal Extension of Human AP Endonuclease 1 In Coordination of Base Excision DNA Repair via Protein–Protein Interactions

Moor, N. A., Васильева, И. А., & Lavrik, O. I. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21093122 · Cited by 18 · see citing works

Roles of DNA damage repair and precise targeted therapy in renal cancer (Review)

Lai, Y., Li, Z., Lu, Z., Zheng, H., Chen, C., Liu, C., Yang, Y., Tang, F., & He, Z. (2022) · Oncology Reports · doi:10.3892/or.2022.8428 · Cited by 17 · see citing works

XRCC1 and DNA strand break repair

Caldecott, K. W. (2003) · DNA repair · doi:10.1016/s1568-7864(03)00118-6 · Cited by 598 · see citing works

Mammalian DNA single‐strand break repair: an X‐ra(y)ted affair

Caldecott, K. W. (2001) · BioEssays · doi:10.1002/bies.1063 · Cited by 175 · see citing works

XRCC1 Stimulates Human Polynucleotide Kinase Activity at Damaged DNA Termini and Accelerates DNA Single-Strand Break Repair

Whitehouse, C. J., Taylor, R., Thistlethwaite, A., Zhang, H., Karimi‐Busheri, F., Lasko, D. D., Weinfeld, M., & Caldecott, K. W. (2001) · Cell · doi:10.1016/s0092-8674(01)00195-7 · Cited by 608 · see citing works

Poly(ADP-ribose) polymerase-1 modulates DNA repair capacity and prevents formation of DNA double strand breaks

Woodhouse, B. C., Dianova, I. I., Parsons, J. L., & Dianov, G. L. (2008) · DNA repair · doi:10.1016/j.dnarep.2008.03.017 · Cited by 107 · see citing works

XRCC1 keeps DNA from getting stranded

Thompson, L. H., & West, M. G. (2000) · Mutation Research/DNA Repair · doi:10.1016/s0921-8777(99)00058-0 · Cited by 444 · see citing works