Repair of Endogenous DNA Damage

Rate of depurination of native deoxyribonucleic acid

Lindahl, T. L., & Nyberg, B. (1972) · Biochemistry · doi:10.1021/bi00769a018 · Cited by 1,558 · see citing works

Quality Control by DNA Repair

Lindahl, T. L., & Wood, R. D. (1999) · Science · doi:10.1126/science.286.5446.1897 · Cited by 1,489 · see citing works

Structural basis for recognition and repair of the endogenous mutagen 8-oxoguanine in DNA

Bruner, S. D., Norman, D. P. G., & Verdine, G. L. (2000) · Nature · doi:10.1038/35002510 · Cited by 972 · see citing works

Accumulation of premutagenic DNA lesions in mice defective in removal of oxidative base damage

Klungland, A., Rosewell, I., Hollenbach, S., Larsen, E., Daly, G., Epe, B., Seeberg, E., Lindahl, T., & Barnes, D. E. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.23.13300 · Cited by 807 · 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

DNA-bound structures and mutants reveal abasic DNA binding by APE1 DNA repair and coordination

Mol, C. D., Izumi, T., MITRA, S. P., & Tainer, J. A. (2000) · Nature · doi:10.1038/35000249 · Cited by 756 · see citing works

Heat-induced deamination of cytosine residues in deoxyribonucleic acid

Lindahl, T. L., & Nyberg, B. (1974) · Biochemistry · doi:10.1021/bi00713a035 · Cited by 749 · 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

The GO system protects organisms from the mutagenic effect of the spontaneous lesion 8-hydroxyguanine (7,8-dihydro-8-oxoguanine)

Michaels, M. L., & Miller, J. H. (1992) · Journal of Bacteriology · doi:10.1128/jb.174.20.6321-6325.1992 · Cited by 693 · see citing works

The thymine glycosylase MBD4 can bind to the product of deamination at methylated CpG sites

Hendrich, B., Hardeland, U., Ng, H., Jiricny, J., & Bird, A. P. (1999) · Nature · doi:10.1038/45843 · Cited by 637 · see citing works

Formation, Prevention, and Repair of DNA Damage by Iron/Hydrogen Peroxide

Henle, E. S., & Linn, S. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.31.19095 · Cited by 582 · see citing works

A sensitive genetic assay for the detection of cytosine deamination: determination of rate constants and the activation energy

Frederico, L. A., Kunkel, T. A., & Shaw, B. R. (1990) · Biochemistry · doi:10.1021/bi00462a015 · Cited by 498 · see citing works

The Human OGG1 Gene: Structure, Functions, and Its Implication in the Process of Carcinogenesis

Boiteux, S., & Radicella, J. P. (2000) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2000.1773 · Cited by 478 · see citing works

The rate of hydrolytic deamination of 5-methylcytosine in double-stranded DNA

Shen, J., Rideout, W. M., & Jones, P. A. (1994) · Nucleic Acids Research · doi:10.1093/nar/22.6.972 · Cited by 458 · 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

Cloning and sequencing a human homolog (hMYH) of the Escherichia coli mutY gene whose function is required for the repair of oxidative DNA damage

Slupska, M. M., Baikalov, C., Luther, W. M., Chiang, J., Wei, Y., & Miller, J. H. (1996) · Journal of Bacteriology · doi:10.1128/jb.178.13.3885-3892.1996 · Cited by 386 · see citing works

Redox-Regulated Recruitment of the Transcriptional Coactivators CREB-Binding Protein and SRC-1 to Hypoxia-Inducible Factor 1α

Carrero, P., Okamoto, K., Coumailleau, P., O’Brien, S. L., Tanaka, H., & Poellinger, L. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.1.402-415.2000 · Cited by 382 · see citing works

The redox and DNA-repair activities of Ref-1 are encoded by nonoverlapping domains.

Xanthoudakis, S., Miao, G. G., & Curran, T. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.1.23 · Cited by 355 · see citing works

Interaction of human apurinic endonuclease and DNA polymerase β in the base excision repair pathway

Bennett, R. A. O., Wilson, D. M., Wong, D., & Demple, B. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.14.7166 · Cited by 350 · see citing works

Mmh / Ogg1 gene inactivation results in accumulation of 8-hydroxyguanine in mice

Minowa, O., Arai, T., Hirano, M., Monden, Y., Nakai, S., Fukuda, M., Itoh, M., Takano, H., Hippou, Y., Aburatani, H., et al. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.050404497 · Cited by 348 · see citing works

Removal of oxygen free-radical-induced 5′,8-purine cyclodeoxynucleosides from DNA by the nucleotide excision-repair pathway in human cells

Kuraoka, I., Bender, C., Romieu, A., Cadet, J., Wood, R. D., & Lindahl, T. L. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.070471597 · Cited by 346 · see citing works

Passing the baton in base excision repair.

Kunkel, T. A., & Wilson, S. H. (2000) · Nature Structural Biology · doi:10.1038/73260 · Cited by 345 · see citing works

The lyase activity of the DNA repair protein β-polymerase protects from DNA-damage-induced cytotoxicity

Sobol, R. W., Prasad, R., Evenski, A. J., Baker, A. E., Yang, X., Horton, J. K., & Wilson, S. H. (2000) · Nature · doi:10.1038/35015598 · Cited by 343 · 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

Uracil-DNA Glycosylase (UNG)-Deficient Mice Reveal a Primary Role of the Enzyme during DNA Replication

Nilsen, H. L., Rosewell, I. R., Robins, P., Skjelbred, C. F., Andersen, S. B., Slupphaug, G., Daly, G., Krokan, H. E., Lindahl, T. L., & Barnes, D. E. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80271-3 · Cited by 320 · see citing works

Functional sites of interaction between release factor RF1 and the ribosome.

Wilson, K. S., Nakamura, Y., Ito, K., & Noller, H. F. (2000) · Nature Structural Biology · doi:10.1038/82818 · Cited by 309 · see citing works

The Oxidative DNA Lesion 8,5′-(S)-Cyclo-2′-deoxyadenosine Is Repaired by the Nucleotide Excision Repair Pathway and Blocks Gene Expression in Mammalian Cells

Brooks, P. J., Wise, D. S., Berry, D. A., Kosmoski, J. V., Smerdon, M. J., Somers, R. L., Mackie, H., Spoonde, A. Y., Ackerman, E. J., Coleman, K. G., et al. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002259200 · Cited by 298 · see citing works

Base Excision Repair of Oxidative DNA Damage Activated by XPG Protein

Klungland, A., Höss, M., Gunz, D., Constantinou, A., Clarkson, S. G., Doetsch, P. W., Bolton, P. H., Wood, R. D., & Lindahl, T. L. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80172-0 · Cited by 291 · see citing works

Highly sensitive apurinic/apyrimidinic site assay can detect spontaneous and chemically induced depurination under physiological conditions.

Nakamura, J., Walker, V. E., Upton, P. B., Chiang, S. Y., Kow, Y. W., & Swenberg, J. A. (1998) · PubMed · Cited by 277 · 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

Cloning and Expression of Human G/T Mismatch-specific Thymine-DNA Glycosylase

Neddermann, P., Gallinari, P., Lettieri, T., SCHMID, D. M., Truong, O., Hsuan, J. J., Wiebauer, K., & Jiricny, J. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.22.12767 · Cited by 259 · 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

The Type of DNA Glycosylase Determines the Base Excision Repair Pathway in Mammalian Cells

Fortini, P., Parlanti, E., Sidorkina, O. M., Laval, J., & Eugenia Dogliotti, Y. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.21.15230 · Cited by 249 · see citing works

Base excision repair deficient mice lacking the Aag alkyladenine DNA glycosylase

Engelward, B. P., Weeda, G., Wyatt, M. D., Broekhof, J. L. M., de Wit, J., Donker, I., Allan, J. M., Gold, B. I., Hoeijmakers, J. H. J., & Samson, L. D. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.24.13087 · Cited by 235 · see citing works

Inactivation of OGG1 increases the incidence of G · C→T · A transversions in Saccharomyces cerevisiae : evidence for endogenous oxidative damage to DNA in eukaryotic cells

Thomas, D., Scot, A. D., Barbey, R., Padula, M., & Boiteux, S. (1997) · Molecular and General Genetics MGG · doi:10.1007/s004380050405 · Cited by 222 · see citing works

Identification of a new uracil-DNA glycosylase family by expression cloning using synthetic inhibitors

Haushalter, K. A., Stukenberg, P. T., Kirschner, M. W., & Verdine, G. L. (1999) · Current Biology · doi:10.1016/s0960-9822(99)80087-6 · Cited by 220 · see citing works

Long Patch Base Excision Repair with Purified Human Proteins

Pascucci, B., Stucki, M., Jónsson, Z. O., Eugenia Dogliotti, Y., & Hübscher, U. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.47.33696 · Cited by 205 · see citing works

Genetic toxicology of oxygen

Joenje, H. (1989) · Mutation Research/DNAging · doi:10.1016/0921-8734(89)90001-5 · Cited by 197 · see citing works

Increased spontaneous mutation and alkylation sensitivity of Escherichia coli strains lacking the ogt O6-methylguanine DNA repair methyltransferase

Rebeck, G. W., & Samson, L. (1991) · Journal of Bacteriology · doi:10.1128/jb.173.6.2068-2076.1991 · Cited by 177 · see citing works

3, N 4 -ethenocytosine, a highly mutagenic adduct, is a primary substrate for Escherichia coli double-stranded uracil-DNA glycosylase and human mismatch-specific thymine-DNA glycosylase

Saparbaev, M. K., & Laval, J. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.15.8508 · Cited by 176 · see citing works

Reconstitution of Proliferating Cell Nuclear Antigen-dependent Repair of Apurinic/Apyrimidinic Sites with Purified Human Proteins

Matsumoto, Y., Kim, K. M., Hurwitz, J., Gary, R. K., Levin, D. S., Tomkinson, A. E., & Park, M. S. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.47.33703 · Cited by 175 · see citing works

A human DNA editing enzyme homologous to the Escherichia coli DnaQ/MutD protein

Höss, M., Robins, P., Naven, T. J. P., Pappin, D., SGOUROS, J. G., & Lindahl, T. L. (1999) · The EMBO Journal · doi:10.1093/emboj/18.13.3868 · Cited by 170 · see citing works

Erratum: DNA-bound structures and mutants reveal abasic DNA binding by APE1 and DNA repair coordination

Mol, C. D., Izumi, T., MITRA, S. P., & Tainer, J. A. (2000) · Nature · doi:10.1038/35006693 · Cited by 161 · see citing works

Mutagenicity in Escherichia coli of the major DNA adduct derived from the endogenous mutagen malondialdehyde

Fink, S. P., Reddy, G. R., & Marnett, L. J. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.16.8652 · Cited by 159 · see citing works

Generation of an endogenous DNA-methylating agent by nitrosation in Escherichia coli

Taverna, P., & Sedgwick, B. (1996) · Journal of Bacteriology · doi:10.1128/jb.178.17.5105-5111.1996 · Cited by 158 · see citing works

The BRCA1 C-terminal domain: structure and function

Huyton, T., Bates, P. A., Zhang, X., Sternberg, M. J. E., & Freemont, P. S. (2000) · Mutation Research/DNA Repair · doi:10.1016/s0921-8777(00)00034-3 · Cited by 147 · see citing works

Transcription coupled repair of 8-oxoguanine in murine cells: The Ogg1 protein is required for repair in nontranscribed sequences but not in transcribed sequences

Page, F. L., Klungland, A., Barnes, D. E., Sarasin, A. R., & Boiteux, S. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.140137297 · Cited by 141 · see citing works

Thermodynamic Consequences of an Abasic Lesion in Duplex DNA Are Strongly Dependent on Base Sequence

Gelfand, C. A., Plum, G. E., Grollman, A. P., Johnson, F., & Breslauer, K. J. (1998) · Biochemistry · doi:10.1021/bi9803372 · Cited by 127 · see citing works

Alkylpurine–DNA–N-Glycosylase Knockout Mice Show Increased Susceptibility to Induction of Mutations by Methyl Methanesulfonate

Elder, R. H., Jansen, J. G., Weeks, R. J., Willington, M. A., Deans, B., Watson, A. J., Mynett, K. J., Bailey, J., Cooper, D. P., Rafferty, J. A., et al. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.10.5828 · Cited by 114 · see citing works

The spectrum of spontaneous mutations in a Saccharomyces cerevisiae uracil-DNA-glycosylase mutant limits the function of this enzyme to cytosine deamination repair

Impellizzeri, K. J., Anderson, B. A., & Burgers, P. (1991) · Journal of Bacteriology · doi:10.1128/jb.173.21.6807-6810.1991 · Cited by 107 · see citing works

DNA specificity enhanced by sequential binding of protein monomers

Kohler, J. J., Metallo, S. J., Schneider, T. L., & Schepartz, A. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.21.11735 · Cited by 105 · see citing works

How do DNA repair proteins locate damaged bases in the genome?

Verdine, G. L., & Bruner, S. D. (1997) · Chemistry & Biology · doi:10.1016/s1074-5521(97)90123-x · Cited by 93 · see citing works

A 55-kDa protein isolated from human cells shows DNA glycosylase activity toward 3, N 4 -ethenocytosine and the G/T mismatch

Hang, B., Medina, M., Fraenkel‐Conrat, H., & Singer, B. A. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.23.13561 · Cited by 81 · see citing works

Single Nucleotide Patch Base Excision Repair Is the Major Pathway for Removal of Thymine Glycol from DNA in Human Cell Extracts

Dianov, G. L., Thybo, T., Dianova, I. I., Lipinski, L. J., & Bohr, V. A. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.16.11809 · Cited by 79 · see citing works

Database of mouse strains carrying targeted mutations in genes affecting cellular responses to DNA damage: version 3

Friedberg, E. C., & Meira, L. B. (1999) · Mutation Research/DNA Repair · doi:10.1016/s0921-8777(98)00068-8 · Cited by 76 · see citing works

Database of mouse strains carrying targeted mutations in genes affecting cellular responses to DNA damage. Version 4

Friedberg, E. C., & Meira, L. B. (2000) · Mutation Research/DNA Repair · doi:10.1016/s0921-8777(00)00006-9 · Cited by 47 · see citing works

Immunolocalization of 8-Oxoguanine in Nutrient-Deprived Mammalian Tissue

Conion, K. A., Grollman, A. P., & Berríos, M. (2000) · Journal of Histotechnology · doi:10.1179/his.2000.23.1.37 · Cited by 11 · see citing works

The DNA-damage response in human biology and disease

Jackson, S. P., & Bartek, J. (2009) · Nature · doi:10.1038/nature08467 · Cited by 6,092 · see citing works

The DNA Damage Response: Making It Safe to Play with Knives

Ciccia, A., & Elledge, S. J. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.09.019 · Cited by 4,368 · see citing works

Mechanisms of DNA damage, repair, and mutagenesis

Chatterjee, N., & Walker, G. C. (2017) · Environmental and Molecular Mutagenesis · doi:10.1002/em.22087 · Cited by 2,039 · see citing works

Gene regulation and DNA damage in the ageing human brain

Lu, T., Pan, Y., Kao, S.-Y., Li, C., Kohane, I., Chan, J., & Yankner, B. A. (2004) · Nature · doi:10.1038/nature02661 · Cited by 1,874 · see citing works

Genomic Instability and Aging-like Phenotype in the Absence of Mammalian SIRT6

Mostoslavsky, R., Chua, K. F., Lombard, D. B., Pang, W. W., Fischer, M. R., Gellon, L., Liu, P., Mostoslavsky, G., Franco, S., Murphy, M. M., et al. (2006) · Cell · doi:10.1016/j.cell.2005.11.044 · Cited by 1,637 · see citing works

Endogenous DNA damage as a source of genomic instability in cancer

Tubbs, A., & Nussenzweig, A. (2017) · Cell · doi:10.1016/j.cell.2017.01.002 · Cited by 1,452 · see citing works

Dynamics of DNA damage response proteins at DNA breaks: a focus on protein modifications

Polo, S. E., & Jackson, S. P. (2011) · Genes & Development · doi:10.1101/gad.2021311 · Cited by 1,092 · see citing works

Role of oxidative stress and DNA damage in human carcinogenesis

Kryston, T. B., Georgiev, A. B., Pissis, P., & Georgakilas, A. G. (2011) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2010.12.016 · Cited by 927 · 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

Targeting DNA damage response pathways in cancer

Groelly, F. J., Fawkes, M., Dagg, R. A., Blackford, A. N., & Tarsounas, M. (2022) · Nature reviews. Cancer · doi:10.1038/s41568-022-00535-5 · Cited by 868 · see citing works

Repair and Genetic Consequences of Endogenous DNA Base Damage in Mammalian Cells

Barnes, D. E., & Lindahl, T. (2004) · Annual Review of Genetics · doi:10.1146/annurev.genet.38.072902.092448 · Cited by 753 · see citing works

Immunoglobulin Isotype Switching Is Inhibited and Somatic Hypermutation Perturbed in UNG-Deficient Mice

Rada, C. A., Williams, G. T., Nilsen, H. L., Barnes, D. E., Lindahl, T. L., & Neuberger, M. S. (2002) · Current Biology · doi:10.1016/s0960-9822(02)01215-0 · Cited by 712 · see citing works

ATM and ATR as therapeutic targets in cancer

Weber, A. M., & Ryan, A. J. (2014) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2014.12.001 · Cited by 644 · see citing works

Eukaryotic Translesion Polymerases and Their Roles and Regulation in DNA Damage Tolerance

Waters, L. S., Minesinger, B. K., Wiltrout, M. E., D'Souza, S., Woodruff, R. V., & Walker, G. C. (2009) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00034-08 · Cited by 591 · see citing works

A Genetic Map of the Response to DNA Damage in Human Cells

Olivieri, M., Cho, T., Álvarez-Quilón, A., Li, K., Schellenberg, M. J., Zimmermann, M., Hustedt, N., Rossi, S. E., Adam, S., Melo, H., et al. (2020) · Cell · doi:10.1016/j.cell.2020.05.040 · Cited by 551 · see citing works

The cancer–natural killer cell immunity cycle

Huntington, N. D., Cursons, J., & Rautela, J. (2020) · Nature reviews. Cancer · doi:10.1038/s41568-020-0272-z · Cited by 570 · see citing works

Chemotherapy Side-Effects: Not All DNA Damage Is Equal

van den Boogaard, W. M. C., Komninos, D. S. J., & Vermeij, W. P. (2022) · Cancers · doi:10.3390/cancers14030627 · Cited by 482 · see citing works

Enzymatic Removal of Ribonucleotides from DNA Is Essential for Mammalian Genome Integrity and Development

Reijns, M. A. M., Rabe, B., Rigby, R. E., Mill, P., Astell, K. R., Lettice, L. A., Boyle, S., Leitch, A., Keighren, M., Kilanowski, F., et al. (2012) · Cell · doi:10.1016/j.cell.2012.04.011 · Cited by 466 · see citing works

Base excision repair: A critical player in many games

Wallace, S. S. (2014) · DNA Repair · doi:10.1016/j.dnarep.2014.03.030 · Cited by 401 · see citing works

DNA repair mechanisms in cancer development and therapy

Torgovnick, A., & Schumacher, B. (2015) · Frontiers in Genetics · doi:10.3389/fgene.2015.00157 · Cited by 403 · see citing works

Redox Signaling by Reactive Electrophiles and Oxidants

Parvez, S., Long, M. J. C., Poganik, J. R., & Aye, Y. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00698 · Cited by 357 · see citing works

Assembly and function of DNA double-strand break repair foci in mammalian cells

Bekker-Jensen, S., & Mailand, N. (2010) · DNA Repair · doi:10.1016/j.dnarep.2010.09.010 · Cited by 338 · see citing works

Chromatin and nucleosome dynamics in DNA damage and repairPreprint

Hauer, M., & Gasser, S. M. (2017) · Genes & Development · doi:10.1101/gad.307702.117 · Cited by 320 · see citing works

8-Oxoguanine: from oxidative damage to epigenetic and epitranscriptional modification

Hahm, J. Y., Park, J., Jang, E.-S., & Chi, S. W. (2022) · Experimental & Molecular Medicine · doi:10.1038/s12276-022-00822-z · Cited by 325 · see citing works

The Unfolded Protein Response: Detecting and Responding to Fluctuations in the Protein-Folding Capacity of the Endoplasmic ReticulumPreprint

Karagöz, G. E., Acosta‐Alvear, D., & Walter, P. (2019) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a033886 · Cited by 302 · see citing works

Oxygen as a friend and enemy: How to combat the mutational potential of 8-oxo-guanine

van Loon, B., Markkanen, E., & Hübscher, U. (2010) · DNA repair · doi:10.1016/j.dnarep.2010.03.004 · Cited by 310 · see citing works

BRCA1 and BRCA2: breast/ovarian cancer susceptibility gene products and participants in DNA double-strand break repair

O'Donovan, P. J., & Livingston, D. M. (2010) · Carcinogenesis · doi:10.1093/carcin/bgq069 · Cited by 296 · see citing works

Functions of PARylation in DNA Damage Repair Pathways

Wei, H., & Yu, X. (2016) · Genomics Proteomics & Bioinformatics · doi:10.1016/j.gpb.2016.05.001 · Cited by 296 · see citing works

Cellular functions of the protein kinase ATM and their relevance to human disease

Lee, J., & Paull, T. T. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00394-2 · Cited by 290 · see citing works

DNA repair mechanisms in plants: crucial sensors and effectors for the maintenance of genome integrity

Bray, C. M., & West, C. E. (2005) · New Phytologist · doi:10.1111/j.1469-8137.2005.01548.x · Cited by 277 · see citing works

The circadian clock in cancer development and therapy

Fu, L., & Kettner, N. M. (2013) · Progress in Molecular Biology and Translational Science · doi:10.1016/b978-0-12-396971-2.00009-9 · Cited by 251 · see citing works

Activation of the ATR kinase by the RPA-binding protein ETAA1

Haahr, P., Hoffmann, S., Tollenaere, M. A. X., Ho, T., Toledo, L. I., Mann, M., Bekker‐Jensen, S., Räschle, M., & Mailand, N. (2016) · Nature Cell Biology · doi:10.1038/ncb3422 · Cited by 255 · see citing works

Aging in a Dish: iPSC-Derived and Directly Induced Neurons for Studying Brain Aging and Age-Related Neurodegenerative Diseases

Mertens, J., Reid, D. A., Lau, S., Kim, Y., & Gage, F. H. (2018) · Annual Review of Genetics · doi:10.1146/annurev-genet-120417-031534 · Cited by 252 · see citing works

Translesion DNA polymerases in eukaryotes: what makes them tick?

Vaisman, A., & Woodgate, R. (2017) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2017.1291576 · Cited by 247 · 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

The role of poly ADP-ribosylation in the first wave of DNA damage response

Liu, C., Vyas, A., Kassab, M. A., Singh, A. K., & Yu, X. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx565 · Cited by 236 · see citing works

8-Oxoguanine DNA glycosylase 1: Beyond repair of the oxidatively modified base lesions

Ba, X., & Boldogh, I. R. (2017) · Redox Biology · doi:10.1016/j.redox.2017.11.008 · Cited by 239 · see citing works

Break dosage, cell cycle stage and DNA replication influence DNA double strand break response

Zierhut, C., & Diffley, J. F. X. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.111 · Cited by 234 · see citing works

Early neuronal accumulation of DNA double strand breaks in Alzheimer’s disease

Shanbhag, N. M., Evans, M. D., Mao, W., Nana, A. L., Seeley, W. W., Adame, A., Rissman, R. A., Masliah, E., & Mucke, L. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0723-5 · Cited by 214 · see citing works

5-formylcytosine and 5-carboxylcytosine reduce the rate and substrate specificity of RNA polymerase II transcription

Kellinger, M. W., Song, C., Chong, J. P. C., Lu, X., He, C., & Wang, D. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2346 · Cited by 228 · see citing works

Oxidized Guanine Base Lesions Function in 8-Oxoguanine DNA Glycosylase-1-mediated Epigenetic Regulation of Nuclear Factor κB-driven Gene Expression

Pan, L., Zhu, B., Hao, W., Zeng, X., Vlahopoulos, S., Hazra, T. K., Hegde, M. L., Radak, Z. O., Bácsi, A., Brasier, A. R., et al. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.751453 · Cited by 196 · see citing works

Excision of deaminated cytosine from the vertebrate genome: role of the SMUG1 uracil–DNA glycosylase

Nilsen, H. L., Haushalter, K. A., Robins, P., Barnes, D. E., Verdine, G. L., & Lindahl, T. L. (2001) · The EMBO Journal · doi:10.1093/emboj/20.15.4278 · Cited by 196 · see citing works

DNA Damage Response and Immune Defense: Links and Mechanisms

Nakad, R., & Schumacher, B. (2016) · Frontiers in Genetics · doi:10.3389/fgene.2016.00147 · Cited by 193 · see citing works

Cancer Drug Discovery and Development

Humphrey, J. S., Price, K., Gupta, E., Baxter, A. R. W., Bird, J., Sonnichsen, D. S., & Naglich, J. G. (2003) · Humana Press eBooks · doi:10.1007/978-1-59259-325-5_21 · Cited by 195 · see citing works

Not breathing is not an option: How to deal with oxidative DNA damage

Markkanen, E. (2017) · DNA repair · doi:10.1016/j.dnarep.2017.09.007 · Cited by 192 · 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

Clusters of Multiple Mutations: Incidence and Molecular Mechanisms

Chan, K., & Gordenin, D. A. (2015) · Annual Review of Genetics · doi:10.1146/annurev-genet-112414-054714 · Cited by 187 · see citing works

Artesunate Induces Oxidative DNA Damage, Sustained DNA Double-Strand Breaks, and the ATM/ATR Damage Response in Cancer Cells

Berdelle, N., Nikolova, T., Quiros, S., Efferth, T., & Kaina, B. (2011) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-11-0534 · Cited by 181 · see citing works

Crosstalk between PTEN/PI3K/Akt Signalling and DNA Damage in the Oocyte: Implications for Primordial Follicle Activation, Oocyte Quality and Ageing

Maidarti, M., Anderson, R. A., & Telfer, E. E. (2020) · Cells · doi:10.3390/cells9010200 · Cited by 180 · see citing works

The Good, the Bad, and the Ugly of ROS: New Insights on Aging and Aging‐Related Diseases from Eukaryotic and Prokaryotic Model Organisms

Santos, A. L., Sinha, S., & Lindner, A. B. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/1941285 · Cited by 168 · see citing works

DNA Repair and Genome Maintenance in Bacillus subtilis

Lenhart, J. S., Schroeder, J. W., Walsh, B. W., & Simmons, L. A. (2012) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.05020-11 · Cited by 165 · see citing works

Autophagy in DNA Damage Response

Czarny, P. L., Pawłowska, E., Białkowska, J., Kaarniranta, K., & Błasiak, J. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms16022641 · Cited by 162 · see citing works

Epigenetic drivers and genetic passengers on the road to cancer

Sawan, C., Vaissière, T., Murr, R., & Herceg, Z. (2008) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2008.03.002 · Cited by 164 · see citing works

Reactive oxygen species and DNA damage response in cancer

Renaudin, X. (2021) · International review of cytology · doi:10.1016/bs.ircmb.2021.04.001 · Cited by 164 · see citing works

DNA replication fidelity and cancer

Preston, B. D., Albertson, T. M., & Herr, A. J. (2010) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2010.10.009 · Cited by 160 · see citing works

The BRCA Tumor Suppressor Network in Chromosome Damage Repair by Homologous Recombination

Zhao, W., Wiese, C., Kwon, Y., Hromas, R., & Sung, P. (2019) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-013118-111058 · Cited by 161 · see citing works

A systematic CRISPR screen defines mutational mechanisms underpinning signatures caused by replication errors and endogenous DNA damage

Zou, X., Koh, C. C., Nanda, A. S., Degasperi, A., Urgo, K., Roumeliotis, T. I., Agu, C. A., Badja, C., Momen, S., Young, J., et al. (2021) · Nature Cancer · doi:10.1038/s43018-021-00200-0 · Cited by 146 · see citing works

The genome-wide effects of ionizing radiation on mutation induction in the mammalian germline

Adewoye, A. B., Lindsay, S., Dubrova, Y. E., & Hurles, M. E. (2015) · Nature Communications · doi:10.1038/ncomms7684 · Cited by 155 · see citing works

Epigenetics, DNA damage, and aging

Soto-Palma, C., Niedernhofer, L., Faulk, C. D., & Dong, X. (2022) · Journal of Clinical Investigation · doi:10.1172/jci158446 · Cited by 112 · see citing works

Human RNF169 is a negative regulator of the ubiquitin-dependent response to DNA double-strand breaks.

Poulsen, M., Lukas, C., Lukas, J., Bekker-Jensen, S., & Mailand, N. (2012) · Journal of Cell Biology · doi:10.1083/jcb.201109100 · Cited by 146 · see citing works

SIRT6 in DNA repair, metabolism and ageing

Lombard, D. B., Schwer, B., Alt, F. W., & Mostoslavsky, R. (2008) · Journal of Internal Medicine · doi:10.1111/j.1365-2796.2007.01902.x · Cited by 146 · see citing works

HELB Is a Feedback Inhibitor of DNA End Resection

Tkáč, J., Xu, G., Adhikary, H., Young, J. T. F., Gallo, D., Escribano‐Diaz, C., Krietsch, J., Orthwein, A., Munro, M., Sol, W., et al. (2016) · Molecular Cell · doi:10.1016/j.molcel.2015.12.013 · Cited by 144 · see citing works

Loss of BRCA1 or BRCA2 markedly increases the rate of base substitution mutagenesis and has distinct effects on genomic deletions

Zámborszky, J., Szikriszt, B., Gervai, J. Z., Pipek, O., Póti, Á., Krzystanek, M., Ribli, D., Szalai-Gindl, J. M., Csabai, I., Szállási, Z., et al. (2016) · Oncogene · doi:10.1038/onc.2016.243 · Cited by 143 · see citing works

Base Excision Repair and its Role in Maintaining Genome Stability

Baute, J., & Depicker, A. (2008) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409230802309905 · Cited by 139 · see citing works

DNA damage–inducible SUMOylation of HERC2 promotes RNF8 binding via a novel SUMO-binding Zinc finger

Danielsen, J. M. R., Povlsen, L. K., Villumsen, B. H., Streicher, W. W., Nilsson, J., Wikström, M., Bekker‐Jensen, S., & Mailand, N. (2012) · The Journal of Cell Biology · doi:10.1083/jcb.201106152 · Cited by 135 · see citing works

Telomere Length and Oxidative Stress and Its Relation with Metabolic Syndrome Components in the Aging

Gavia-García, G., Rosado-Pérez, J., Arista-Ugalde, T. L., Aguíñiga-Sánchez, I., Santiago‐Osorio, E., & Mendoza-Núñez, V. M. (2021) · Biology · doi:10.3390/biology10040253 · Cited by 141 · see citing works

Combination Platinum-based and DNA Damage Response-targeting Cancer Therapy: Evolution and Future Directions

Basourakos, S. P., Li, L., Aparicio, A. M., Corn, P. G., Kim, J., & Thompson, T. C. (2016) · Current Medicinal Chemistry · doi:10.2174/0929867323666161214114948 · Cited by 133 · see citing works

DNA repair in mammalian embryos

Jaroudi, S., & SenGupta, S. B. (2006) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2006.09.002 · Cited by 129 · 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

Mechanisms of DNA damage-mediated neurotoxicity in neurodegenerative disease

Welch, G., & Tsai, L. (2022) · The EMBO Reports · doi:10.15252/embr.202154217 · Cited by 129 · see citing works

The synthetic lethality of targeting cell cycle checkpoints and PARPs in cancer treatment

Li, S., Wang, L., Wang, Y., Zhang, C., Hong, Z., & Han, Z. (2022) · Journal of Hematology & Oncology · doi:10.1186/s13045-022-01360-x · Cited by 133 · see citing works

Going beyond five bases in DNA sequencing

Korlach, J., & Turner, S. W. (2012) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2012.04.002 · Cited by 125 · see citing works

The Role of 8-Oxoguanine DNA Glycosylase-1 in Inflammation

Ba, X., Aguilera-Aguirre, L., Rashid, Q. T. A., Bácsi, A., Radak, Z. O., Sur, S. A., Hosoki, K., Hegde, M. L., & Boldogh, I. R. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms150916975 · Cited by 123 · see citing works

Conserved Structural Chemistry for Incision Activity in Structurally Non-homologous Apurinic/Apyrimidinic Endonuclease APE1 and Endonuclease IV DNA Repair Enzymes

Tsutakawa, S. E., Shin, D. S., Mol, C. D., Izumi, T., Arvai, A. S., Mantha, A. K., Szczęsny, B., Ivanov, I. N., Hosfield, D. J., Maiti, B., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.422774 · Cited by 118 · see citing works

The capacity of oocytes for DNA repair

Stringer, J. M., Winship, A., Liew, S. H., & Hutt, K. J. (2018) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-018-2833-9 · Cited by 117 · see citing works

The Intra-S Checkpoint Responses to DNA Damage

Iyer, D., & Rhind, N. (2017) · Genes · doi:10.3390/genes8020074 · Cited by 113 · see citing works

DNA Repair Pathways and Mechanisms

Dexheimer, T. (2013) · Springer eBooks · doi:10.1007/978-94-007-4590-2_2 · Cited by 110 · see citing works

Synthetically Lethal Interactions of ATM, ATR, and DNA-PKcs

Kantidze, O. L., Velichko, A. K., Luzhin, A. V., Petrova, N. V., & Razin, S. V. (2018) · Trends in cancer · doi:10.1016/j.trecan.2018.09.007 · Cited by 111 · see citing works

Single Qdot-labeled glycosylase molecules use a wedge amino acid to probe for lesions while scanning along DNA

Dunn, A. R., Kad, N. M., Nelson, S. R., Warshaw, D. M., & Wallace, S. S. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr459 · Cited by 113 · see citing works

Current Perspective in the Discovery of Anti-aging Agents from Natural Products

Ding, A., Zheng, S., Huang, X., Xing, T.-K., Wu, G.-S., Sun, H., Qi, S., & Luo, H. (2017) · Natural Products and Bioprospecting · doi:10.1007/s13659-017-0135-9 · Cited by 111 · see citing works

Chromatin Dynamics in Genome Stability: Roles in Suppressing Endogenous DNA Damage and Facilitating DNA Repair

Nair, N., Shoaib, M., & Sørensen, C. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18071486 · Cited by 98 · see citing works

Incorporation of dUMP into DNA is a major source of spontaneous DNA damage, while excision of uracil is not required for cytotoxicity of fluoropyrimidines in mouse embryonic fibroblasts

Andersen, S. B. (2004) · Carcinogenesis · doi:10.1093/carcin/bgh347 · Cited by 111 · see citing works

Prevention of Treacher Collins syndrome craniofacial anomalies in mouse models via maternal antioxidant supplementation

Sakai, D., Dixon, J., Achilleos, A., Dixon, M. J., & Trainor, P. A. (2016) · Nature Communications · doi:10.1038/ncomms10328 · Cited by 112 · see citing works

Inflammation, DNA Damage, Helicobacter pylori and Gastric Tumorigenesis

Kalisperati, P., Spanou, E., Pateras, I. S., Korkolopoulou, P. A., Varvarigou, A. A., Karavokyros, I., Gorgoulis, V. G., Vlachoyiannopoulos, P. G., & Sougioultzis, S. (2017) · Frontiers in Genetics · doi:10.3389/fgene.2017.00020 · Cited by 108 · see citing works

Occupational pesticide exposure, impaired DNA repair, and diseases

Kaur, R., & Kaur, K. (2018) · Indian Journal of Occupational and Environmental Medicine · doi:10.4103/ijoem.ijoem_45_18 · Cited by 110 · see citing works

The Intertwined Roles of Transcription and Repair Proteins

Fong, Y. W., Cattoglio, C., & Tjian, R. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.10.018 · Cited by 106 · see citing works

The roles of base excision repair enzyme OGG1 in gene expression

Wang, R., Hao, W., Pan, L., Boldogh, I. R., & Ba, X. (2018) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-018-2887-8 · Cited by 106 · see citing works

The ubiquitin‐ and SUMO‐dependent signaling response to DNA double‐strand breaks

Bekker‐Jensen, S., & Mailand, N. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.05.056 · Cited by 105 · see citing works

qDRIP: a method to quantitatively assess RNA–DNA hybrid formation genome-wide

Crossley, M. P., Bocek, M. J., Hamperl, S., Swigut, T., & Cimprich, K. A. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa500 · Cited by 102 · see citing works

The Structural Location of DNA Lesions in Nucleosome Core Particles Determines Accessibility by Base Excision Repair Enzymes

Rodriguez, Y., & Smerdon, M. J. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.441444 · Cited by 98 · see citing works

Two glycosylase families diffusively scan DNA using a wedge residue to probe for and identify oxidatively damaged bases

Nelson, S. R., Dunn, A. R., Kathe, S. D., Warshaw, D. M., & Wallace, S. S. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1400386111 · Cited by 97 · see citing works

A Role for the Host DNA Damage Response in Hepatitis B Virus cccDNA Formation—and Beyond?

Schreiner, S., & Nassal, M. (2017) · Viruses · doi:10.3390/v9050125 · Cited by 97 · 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

DNA Break Mapping Reveals Topoisomerase II Activity Genome-Wide

Baranello, L., Kouzine, F., Wójtowicz, D., Cui, K., Przytycka, T. M., Zhao, K., & Levens, D. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms150713111 · Cited by 92 · see citing works

Sirtuin 6: a review of biological effects and potential therapeutic properties

Beauharnois, J. M., Bolívar, B. E., & Welch, J. T. (2013) · Molecular BioSystems · doi:10.1039/c3mb00001j · Cited by 90 · see citing works

Targeting cancer-cell mitochondria and metabolism to improve radiotherapy response

McCann, E., O'Sullivan, J. N., & Marcone, S. (2020) · Translational Oncology · doi:10.1016/j.tranon.2020.100905 · Cited by 89 · see citing works

Chemical Insights into Oxidative and Nitrative Modifications of DNA

Andrés, C. M. C., de la Lastra, J. M. P., Andrés, C., Plou, F. J., & Pérez‐Lebeña, E. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242015240 · Cited by 93 · see citing works

Towards a comprehensive view of 8-oxo-7,8-dihydro-2’-deoxyguanosine: Highlighting the intertwined roles of DNA damage and epigenetics in genomic instability

Gorini, F., Scala, G., Cooke, M. S., Majello, B., & Amente, S. (2020) · DNA repair · doi:10.1016/j.dnarep.2020.103027 · Cited by 88 · see citing works

Revolutionizing DNA repair research and cancer therapy with CRISPR–Cas screens

Awwad, S. W., Serrano-Benítez, A., Thomas, J. C., Gupta, V., & Jackson, S. P. (2023) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-022-00571-x · Cited by 87 · see citing works

Direct Detection and Sequencing of Damaged DNA Bases

Clark, T. A., Spittle, K. E., Turner, S. W., & Korlach, J. (2011) · Genome Integrity · doi:10.1186/2041-9414-2-10 · Cited by 88 · see citing works

Repair and Genetic Consequences of Endogenous DNA Base Damage in Mammalian Cells

Barnes, D. E., & Lindahl, T. (2004) · Annual Review of Genetics · doi:10.1146/annurev.genet.38.072902.092448 · Cited by 753 · see citing works

The Croonian Lecture, 1996: Endogenous damage to DNA

Lindahl, T. (1996) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.1996.0139 · Cited by 97 · see citing works

Suppression of spontaneous mutagenesis in human cells by DNA base excision–repair

Lindahl, T. L. (2000) · Mutation Research/Reviews in Mutation Research · doi:10.1016/s1383-5742(00)00024-7 · Cited by 213 · see citing works

Why Is DNA Double Stranded? The Discovery of DNA Excision Repair Mechanisms

Strauss, B. S. (2018) · Genetics · doi:10.1534/genetics.118.300958 · Cited by 11 · see citing works

Repair Enzyme suggested by Mammalian Endonuclease Activity specific for Ultraviolet-irradiated DNA

Brent, T. P. (1972) · Nature New Biology · doi:10.1038/newbio239172a0 · Cited by 51 · see citing works