DNA glycosylases: In DNA repair and beyond

Conversion of 5-Methylcytosine to 5-Hydroxymethylcytosine in Mammalian DNA by MLL Partner TET1

Tahiliani, M., Koh, K. P., Shen, Y., Pastor, W. A., Bandukwala, H., Brudno, Y., Agarwal, S., Iyer, L. M., Liu, D. R., Aravind, L., et al. (2009) · Science · doi:10.1126/science.1170116 · Cited by 5,836 · see citing works

DNA Repair and Mutagenesis

Friedberg, E. C., Walker, G. C., Siede, W., Wood, R. D., Schultz, R. A., & Ellenberger, T. (2005) · doi:10.1128/9781555816704 · Cited by 5,683 · see citing works

Class Switch Recombination and Hypermutation Require Activation-Induced Cytidine Deaminase (AID), a Potential RNA Editing Enzyme

Muramatsu, M., Kinoshita, K., Fagarasan, S., Yamada, S., Shinkai, Y., & Honjo, T. (2000) · Cell · doi:10.1016/s0092-8674(00)00078-7 · Cited by 3,475 · see citing works

Tet proteins can convert 5-methylcytosine to 5-formylcytosine and 5-carboxylcytosine

Ito, S., Shen, L., Dai, Q., Wu, S. C., Collins, L. B., Swenberg, J. A., He, C., & Zhang, Y. (2011) · Science · doi:10.1126/science.1210597 · Cited by 3,451 · see citing works

Tet-Mediated Formation of 5-Carboxylcytosine and Its Excision by TDG in Mammalian DNA

He, Y., Li, B.-Z., Li, Z., Liu, P., Wang, Y., Tang, Q., Ding, J., Jia, Y., Chen, Z., Li, L., et al. (2011) · Science · doi:10.1126/science.1210944 · Cited by 2,776 · see citing works

Role of Tet proteins in 5mC to 5hmC conversion, ES-cell self-renewal and inner cell mass specification

Ito, S., D’Alessio, A. C., Taranova, O., Hong, K., Sowers, L. C., & Zhang, Y. (2010) · Nature · doi:10.1038/nature09303 · Cited by 2,542 · see citing works

Highly Integrated Single-Base Resolution Maps of the Epigenome in Arabidopsis

Lister, R., O’Malley, R. C., Tonti‐Filippini, J., Gregory, B. D., Berry, C. C., Millar, A. H., & Ecker, J. R. (2008) · Cell · doi:10.1016/j.cell.2008.03.029 · Cited by 2,424 · 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

Inherited variants of MYH associated with somatic G:C→T:A mutations in colorectal tumors

Tassan, N. A. A., Chmiel, N. H., Maynard, J. H., Fleming, N. I., Livingston, A. L., Williams, G. T., Hodges, A., Davies, D. R., David, S. S., Sampson, J. R., et al. (2002) · Nature Genetics · doi:10.1038/ng828 · Cited by 1,392 · see citing works

Identification and Characterization of a Family of Mammalian Methyl-CpG Binding Proteins

Hendrich, B., & Bird, A. P. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.11.6538 · Cited by 1,352 · see citing works

Demethylation of the zygotic paternal genome

Mayer, W., Niveleau, A., Walter, J., Fundele, R. H., & Haaf, T. (2000) · Nature · doi:10.1038/35000656 · Cited by 1,330 · see citing works

Diffusion-driven mechanisms of protein translocation on nucleic acids. 1. Models and theory

Berg, O. G., Winter, R. B., & von Hippel, P. H. (1981) · Biochemistry · doi:10.1021/bi00527a028 · Cited by 1,305 · see citing works

DNA Deamination Mediates Innate Immunity to Retroviral Infection

Harris, R. S., Bishop, K. N., Sheehy, A. M., Craig, H. M., Petersen‐Mahrt, S. K., Watt, I. N., Neuberger, M. S., & Malim, M. H. (2003) · Cell · doi:10.1016/s0092-8674(03)00423-9 · Cited by 1,267 · see citing works

Covalent Modification of DNA Regulates Memory Formation

Miller, C. A., & Sweatt, J. D. (2007) · Neuron · doi:10.1016/j.neuron.2007.02.022 · Cited by 1,180 · see citing works

Temporal and regional changes in DNA methylation in the embryonic, extraembryonic and germ cell lineages during mouse embryo development

Monk, M., Boubelı́k, M., & Lehnert, S. A. (1987) · Development · doi:10.1242/dev.99.3.371 · Cited by 1,100 · see citing works

Active demethylation of the paternal genome in the mouse zygote

Oswald, J., Engemann, S., Lane, N., Mayer, W., Olek, A., Fundele, R. H., Dean, W., Reik, W., & Walter, J. (2000) · Current Biology · doi:10.1016/s0960-9822(00)00448-6 · Cited by 983 · see citing works

Conservation of methylation reprogramming in mammalian development: Aberrant reprogramming in cloned embryos

Dean, W., Santos, F., Stojković, M., Zakhartchenko, V., Walter, J., Wolf, E., & Reik, W. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.241522698 · Cited by 973 · 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

The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif

Sheehy, A. M., Gaddis, N., & Malim, M. H. (2003) · Nature Medicine · doi:10.1038/nm945 · Cited by 961 · see citing works

Cyclical DNA methylation of a transcriptionally active promoter

Métivier, R., Gallais, R., Tiffoche, C., Péron, C. L., Jurkowska, R., Carmouche, R. P., Ibberson, D., Baráth, P., Demay, F., Reid, G., et al. (2008) · Nature · doi:10.1038/nature06544 · Cited by 942 · see citing works

Neuronal Activity–Induced Gadd45b Promotes Epigenetic DNA Demethylation and Adult Neurogenesis

Dengke, K., Jang, M., Guo, J. U., Kitabatake, Y., Chang, M.-L., Pow-anpongkul, N., Flavell, R. A., Lu, B., Ming, G., & Song, H. (2009) · Science · doi:10.1126/science.1166859 · Cited by 929 · see citing works

Genome-wide erasure of DNA methylation in mouse primordial germ cells is affected by AID deficiency

Popp, C., Dean, W., Feng, S., Cokus, S. J., Andrews, S., Pellegrini, M. A., Jacobsen, S. E., & Reik, W. (2010) · Nature · doi:10.1038/nature08829 · Cited by 860 · see citing works

DNA glycosylases in the base excision repair of DNA

Krokan, H. E., Standal, R., & Slupphaug, G. (1997) · Biochemical Journal · doi:10.1042/bj3250001 · Cited by 859 · see citing works

Thymine DNA Glycosylase Can Rapidly Excise 5-Formylcytosine and 5-Carboxylcytosine

Maiti, A., & Drohat, A. C. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.c111.284620 · Cited by 825 · see citing works

Thymine DNA glycosylase is essential for active DNA demethylation by linked deamination-base excision repair

Cortellino, S., Xu, J., Sannai, M., Moore, R., Caretti, E., Cigliano, A., Le Coz, M., Devarajan, K., Wessels, A., Soprano, D., et al. (2011) · Cell · doi:10.1016/j.cell.2011.06.020 · Cited by 809 · 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

Oxidative demethylation by Escherichia coli AlkB directly reverts DNA base damage

Trewick, S. C., Henshaw, T. F., Hausinger, R. P., Lindahl, T. L., & Sedgwick, B. (2002) · Nature · doi:10.1038/nature00908 · Cited by 762 · see citing works

Active DNA Demethylation Mediated by DNA Glycosylases

Zhu, J. (2009) · Annual Review of Genetics · doi:10.1146/annurev-genet-102108-134205 · Cited by 746 · see citing works

Developmental pattern of gene-specific DNA methylation in the mouse embryo and germ line.Preprint

Kafri, T., Ariel, M. S., Brandeis, M., Shemer, R., Urven, L. E., McCarrey, J. R., Cedar, H., & Razin, A. (1992) · Genes & Development · doi:10.1101/gad.6.5.705 · Cited by 736 · 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

Transient cyclical methylation of promoter DNA

Kangaspeska, S., Stride, B. D., Métivier, R., Polycarpou-Schwarz, M., Ibberson, D., Carmouche, R. P., Beneš, V., Gannon, F., & Reid, G. (2008) · Nature · doi:10.1038/nature06640 · Cited by 682 · see citing works

Reprogramming towards pluripotency requires AID-dependent DNA demethylation

Bhutani, N., Brady Jennifer, J., Damian, M., Sacco, A., Corbel, S. Y., & Blau, H. M. (2009) · Nature · doi:10.1038/nature08752 · Cited by 676 · see citing works

DNA Demethylation in Zebrafish Involves the Coupling of a Deaminase, a Glycosylase, and Gadd45

Rai, K., Huggins, I. J., James, S. R., Karpf, A. R., Jones, D. A., & Cairns, B. R. (2008) · Cell · doi:10.1016/j.cell.2008.11.042 · Cited by 657 · see citing works

DNA Repair in Mammalian Cells

Robertson, A. B., Klungland, A., Rognes, T., & Leiros, I. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-8736-z · Cited by 652 · see citing works

Human uracil–DNA glycosylase deficiency associated with profoundly impaired immunoglobulin class-switch recombination

Imai, K., Slupphaug, G., Lee, W., Revy, P., Nonoyama, S., Catalan, N., Yel, L., Forveille, M., Kavli, B., Krokan, H. E., et al. (2003) · Nature Immunology · doi:10.1038/ni974 · Cited by 633 · see citing works

AlkB-mediated oxidative demethylation reverses DNA damage in Escherichia coli

Falnes, P. Ø., Johansen, R., & Seeberg, E. C. (2002) · Nature · doi:10.1038/nature01048 · Cited by 617 · 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

Cloning and characterization of hOGG1 , a human homolog of the OGG1 gene of Saccharomyces cerevisiae

Radicella, J. P., Dhérin, C., Desmaze, C., Fox, M. S., & Boiteux, S. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.15.8010 · Cited by 595 · see citing works

Altering the pathway of immunoglobulin hypermutation by inhibiting uracil-DNA glycosylase

Noia, J. M. D., & Neuberger, M. S. (2002) · Nature · doi:10.1038/nature00981 · Cited by 589 · see citing works

A nucleotide-flipping mechanism from the structure of human uracil–DNA glycosylase bound to DNA

Slupphaug, G., Mol, C. D., Kavli, B., Arvai, A. S., Krokan, H. E., & Tainer, J. A. (1996) · Nature · doi:10.1038/384087a0 · Cited by 581 · see citing works

Biochemistry and biology of mammalian DNA methyltransferases

Hermann, A., Gowher, H., & Jeltsch, A. (2004) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-004-4201-1 · Cited by 536 · see citing works

DNA demethylation in the Arabidopsis genome

Penterman, J. N., Zilberman, D., Huh, J. H., Ballinger, T. J., Henikoff, S., & Fischer, R. L. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0701861104 · Cited by 527 · see citing works

Endogenous Cytosine Damage Products Alter the Site Selectivity of Human DNA Maintenance Methyltransferase DNMT1

Valinluck, V., & Sowers, L. C. (2007) · Cancer Research · doi:10.1158/0008-5472.can-06-3123 · Cited by 502 · see citing works

Identification and characterization of a human DNA glycosylase for repair of modified bases in oxidatively damaged DNA

Hazra, T. K., Izumi, T., Boldogh, I. R., Imhoff, B. R., Kow, Y. W., Jaruga, P., Dizdaroğlu, M., & MITRA, S. P. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.062053799 · Cited by 497 · see citing works

Base excision repair initiation revealed by crystal structures and binding kinetics of human uracil‐DNA glycosylase with DNA

Parikh, S. S., Mol, C. D., Slupphaug, G., Bharati, S., Krokan, H. E., & Tainer, J. A. (1998) · The EMBO Journal · doi:10.1093/emboj/17.17.5214 · Cited by 493 · see citing works

Evolution of the AID/APOBEC Family of Polynucleotide (Deoxy)cytidine Deaminases

Conticello, S. G., Thomas, C. J. F., Petersen‐Mahrt, S. K., & Neuberger, M. S. (2004) · Molecular Biology and Evolution · doi:10.1093/molbev/msi026 · Cited by 489 · see citing works

Cloning and expression in Escherichia coli of the gene for human tumour necrosis factor

Shirai, T., Yamaguchi, H., Ito, H., Todd, C. W., & Wallace, R. B. (1985) · Nature · doi:10.1038/313803a0 · Cited by 458 · see citing works

Selective, stable demethylation of the interleukin-2 gene enhances transcription by an active process

Bruniquel, D., & Schwartz, R. H. (2003) · Nature Immunology · doi:10.1038/ni887 · Cited by 457 · 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

Cloning of a yeast 8-oxoguanine DNA glycosylase reveals the existence of a base-excision DNA-repair protein superfamily

Nash, H. M., Bruner, S. D., Schärer, O. D., Kawate, T., Addona, T. A., Spooner, E., Lane, W. S., & Verdine, G. L. (1996) · Current Biology · doi:10.1016/s0960-9822(02)00641-3 · Cited by 435 · see citing works

Stimulation of human 8-oxoguanine-DNA glycosylase by AP-endonuclease: potential coordination of the initial steps in base excision repair

Hill, J. W. (2001) · Nucleic Acids Research · doi:10.1093/nar/29.2.430 · Cited by 411 · see citing works

Biallelic germline mutations in MYH predispose to multiple colorectal adenoma and somatic G:C->T:A mutations

Jones, S. (2002) · Human Molecular Genetics · doi:10.1093/hmg/11.23.2961 · Cited by 401 · see citing works

The structural basis of specific base-excision repair by uracil–DNA glycosylase

Savva, R., McAuley-Hecht, K. E., Brown, T. P., & Pearl, L. H. (1995) · Nature · doi:10.1038/373487a0 · Cited by 397 · see citing works

Prediction of novel families of enzymes involved in oxidative and other complex modifications of bases in nucleic acids

Iyer, L. M., Tahiliani, M., Rao, A., & Aravind, L. (2009) · Cell Cycle · doi:10.4161/cc.8.11.8580 · Cited by 397 · see citing works

Embryonic lethal phenotype reveals a function of TDG in maintaining epigenetic stability

Cortázar, D., Kunz, C., Selfridge, J., Lettieri, T., Saito, Y., MacDougall, E., Wirz, A., Schuermann, D., Jacobs, A. L., Siegrist, F., et al. (2011) · Nature · doi:10.1038/nature09672 · Cited by 389 · see citing works

Cloning and expression in Escherichia coli of the OGG1 gene of Saccharomyces cerevisiae, which codes for a DNA glycosylase that excises 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine.

van der Kemp, P. A., Thomas, D., Barbey, R., de Oliveira, R. C., & Boiteux, S. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.11.5197 · Cited by 365 · see citing works

Hot Spot Focusing of Somatic Hypermutation in MSH2-Deficient Mice Suggests Two Stages of Mutational Targeting

Rada, C. A., Ehrenstein, M. R., Neuberger, M. S., & Milstein, C. (1998) · Immunity · doi:10.1016/s1074-7613(00)80595-6 · Cited by 357 · see citing works

Crystal structure and mutational analysis of human uracil-DNA glycosylase: Structural basis for specificity and catalysis

Mol, C. D., Arvai, A. S., Slupphaug, G., Kavli, B., Alseth, I., Krokan, H. E., & Tainer, J. A. (1995) · Cell · doi:10.1016/0092-8674(95)90290-2 · Cited by 351 · see citing works

hUNG2 Is the Major Repair Enzyme for Removal of Uracil from U:A Matches, U:G Mismatches, and U in Single-stranded DNA, with hSMUG1 as a Broad Specificity Backup

Kavli, B., Sundheim, O., Akbari, M., Otterlei, M., Nilsen, H. L., Skorpen, F., Aas, P. A., Hagen, L., Krokan, H. E., & Slupphaug, G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207107200 · Cited by 346 · see citing works

Structure of a repair enzyme interrogating undamaged DNA elucidates recognition of damaged DNA

Banerjee, A., Yang, W., Karplus, M., & Verdine, G. L. (2005) · Nature · doi:10.1038/nature03458 · 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

Repair of Oxidized Bases in DNA Bubble Structures by Human DNA Glycosylases NEIL1 and NEIL2

Hong, D., MITRA, S. P., & Hazra, T. K. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m308658200 · Cited by 344 · 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

Nonspecifically bound proteins spin while diffusing along DNA

Blainey, P. C., Luo, G., Kou, S. C., Mangel, W. F., Verdine, G. L., Bagchi, B., & Xie, X. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1716 · Cited by 329 · see citing works

Enhanced CpG Mutability and Tumorigenesis in MBD4-Deficient Mice

Millar, C. B., Guy, J., Sansom, O. J., Selfridge, J., MacDougall, E., Hendrich, B., Keightley, P. D., Bishop, S. M., Clarke, A. R., & Bird, A. P. (2002) · Science · doi:10.1126/science.1073354 · Cited by 328 · see citing works

MutY catalytic core, mutant and bound adenine structures define specificity for DNA repair enzyme superfamily

Guan, Y., Manuel, R. C., Arvai, A. S., Parikh, S. S., Mol, C. D., Miller, J. H., Lloyd, R. S., & Tainer, J. A. (1998) · Nature Structural Biology · doi:10.1038/4168 · Cited by 325 · see citing works

A mammalian DNA repair enzyme that excises oxidatively damaged guanines maps to a locus frequently lost in lung cancer

Lu, R., Nash, H. M., & Verdine, G. L. (1997) · Current Biology · doi:10.1016/s0960-9822(06)00187-4 · Cited by 323 · see citing works

Modification of the human thymine‐DNA glycosylase by ubiquitin‐like proteins facilitates enzymatic turnover

Hardeland, U., Steinacher, R., Jiricny, J., & Schär, P. (2002) · The EMBO Journal · doi:10.1093/emboj/21.6.1456 · Cited by 320 · 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

Nuclear and mitochondrial uracil-DNA glycosylases are generated by alternative splicing and transcription from different positions in the UNG gene

Nilsen, H. L., Otterlei, M., Haug, T., Steinsbekk, K. S., Hernes, T. A. N., Skorpen, F., & Krokan, H. E. (1997) · Nucleic Acids Research · doi:10.1093/nar/25.4.750 · Cited by 314 · 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

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

DNA demethylation is necessary for the epigenetic reprogramming of somatic cell nuclei

Simonsson, S., & Gurdon, J. B. (2004) · Nature Cell Biology · doi:10.1038/ncb1176 · Cited by 306 · see citing works

Atomic Structure of the DNA Repair [4Fe-4S] Enzyme Endonuclease III

Kuo, C.-F., McRee, D. E., Fisher, C. L., O’Handley, S., Cunningham, R. P., & Tainer, J. A. (1992) · Science · doi:10.1126/science.1411536 · Cited by 289 · see citing works

Association of CBP/p300 Acetylase and Thymine DNA Glycosylase Links DNA Repair and Transcription

Tini, M., Benecke, A., Um, S.-J., Torchia, J., Evans, R. M., & Chambon, P. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00453-7 · Cited by 285 · see citing works

Human DNA glycosylases of the bacterial Fpg/MutM superfamily: an alternative pathway for the repair of 8-oxoguanine and other oxidation products in DNA

Morland, I. (2002) · Nucleic Acids Research · doi:10.1093/nar/gkf618 · Cited by 284 · see citing works

APOBEC-mediated viral restriction: not simply editing?

Holmes, R. K., Malim, M. H., & Bishop, K. N. (2007) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2007.01.004 · Cited by 278 · see citing works

MED1, a novel human methyl-CpG-binding endonuclease, interacts with DNA mismatch repair protein MLH1

Bellacosa, A., Cicchillitti, L., Schepis, F., Riccio, A., Yeung, A. T., Matsumoto, Y., Golemis, E. A., Genuardi, M., & Neri, G. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.7.3969 · Cited by 269 · see citing works

Excision of oxidatively damaged DNA bases by the human alpha-hOgg1 protein and the polymorphic alpha-hOgg1(Ser326Cys) protein which is frequently found in human populations

Dhérin, C. (1999) · Nucleic Acids Research · doi:10.1093/nar/27.20.4001 · Cited by 260 · 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

Human Thymine DNA Glycosylase Binds to Apurinic Sites in DNA but Is Displaced by Human Apurinic Endonuclease 1

Waters, T. R., Gallinari, P., Jiricny, J., & SWANN, P. F. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.1.67 · Cited by 253 · see citing works

Crystal Structure of a G:T/U Mismatch-Specific DNA Glycosylase

Barrett, T. E., Savva, R., Panayotou, G., Barlow, T., Brown, T., Jiricny, J., & Pearl, L. H. (1998) · Cell · doi:10.1016/s0092-8674(00)80904-6 · Cited by 248 · see citing works

The metabolic syndrome resulting from a knockout of the NEIL1 DNA glycosylase

Vartanian, V. L., Lowell, B., Minko, I. G., Wood, T. G., Ceci, J. D., George, S., Ballinger, S. W., Corless, C. L., McCullough, A. K., & Lloyd, R. S. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0507444103 · Cited by 248 · 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

Crystal structure of thymine DNA glycosylase conjugated to SUMO-1

Baba, D., Maita, N., Jee, J.-G., Uchimura, Y., Saitoh, H., Sugasawa, K., Hanaoka, F., Tochio, H., Hiroaki, H., & Shirakawa, M. (2005) · Nature · doi:10.1038/nature03634 · Cited by 232 · see citing works

A Back-up Glycosylase in Nth1 Knock-out Mice Is a Functional Nei (Endonuclease VIII) Homologue

Takao, M., Kanno, S., Kobayashi, K., Zhang, Q.-M., Yonei, S., van der Horst, G. T. J., & Yasui, A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206884200 · Cited by 226 · 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

Endonuclease III is an iron-sulfur protein

Cunningham, R. P., Asahara, H., Bank, J. F., Scholes, C. P., Salerno, J. C., Surerus, K. K., Münck, E., McCracken, J., Peisach, J., & Emptage, M. H. (1989) · Biochemistry · doi:10.1021/bi00436a049 · Cited by 221 · 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

A new class of uracil-DNA glycosylases related to human thymine-DNA glycosylase

Gallinari, P., & Jiricny, J. (1996) · Nature · doi:10.1038/383735a0 · Cited by 217 · see citing works

Human Immunodeficiency Virus Type 1 Vpr Induces the Degradation of the UNG and SMUG Uracil-DNA Glycosylases

Schröfelbauer, B., Yu, Q., Zeitlin, S. G., & Landau, N. R. (2005) · Journal of Virology · doi:10.1128/jvi.79.17.10978-10987.2005 · Cited by 216 · see citing works

The mouse ortholog of NEIL3 is a functional DNA glycosylase in vitro and in vivo

Liu, M., Bandaru, V., Bond, J. P., Jaruga, P., Zhao, X., Christov, P. P., Burrows, C. J., Rizzo, C. J., Dizdaroğlu, M., & Wallace, S. S. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0908307107 · Cited by 203 · see citing works

Enzymatic capture of an extrahelical thymine in the search for uracil in DNA

Parker, J. B., Bianchet, M. A., Krosky, D. J., Friedman, J. I., Amzel, L. M., & Stivers, J. T. (2007) · Nature · doi:10.1038/nature06131 · Cited by 200 · see citing works

The enigmatic thymine DNA glycosylase

Cortázar, D., Kunz, C., Saito, Y., Steinacher, R., & Schär, P. (2006) · DNA repair · doi:10.1016/j.dnarep.2006.10.013 · Cited by 198 · see citing works

Base J: Discovery, Biosynthesis, and Possible Functions

Borst, P., & Sabatini, R. S. (2008) · Annual Review of Microbiology · doi:10.1146/annurev.micro.62.081307.162750 · Cited by 198 · see citing works

MSH2–MSH6 stimulates DNA polymerase η, suggesting a role for A:T mutations in antibody genes

Wilson, T., Vaisman, A., Martomo, S. A., Sullivan, P., Lan, L., Hanaoka, F., Yasui, A., Woodgate, R., & Gearhart, P. J. (2005) · The Journal of Experimental Medicine · doi:10.1084/jem.20042066 · Cited by 196 · see citing works

Characterization of a Mammalian Homolog of the Escherichia coli MutY Mismatch Repair Protein

McGoldrick, J. P., Yeh, Y.-C., Solomon, M. S., Essigmann, J. M., & Lu, A.-L. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.2.989 · Cited by 195 · see citing works

Somatic Hypermutation in Muts Homologue (Msh)3-, Msh6-, and Msh3/Msh6-Deficient Mice Reveals a Role for the Msh2–Msh6 Heterodimer in Modulating the Base Substitution Pattern

Wiesendanger, M., Kneitz, B., Edelmann, W., & Scharff, M. D. (2000) · The Journal of Experimental Medicine · doi:10.1084/jem.191.3.579 · Cited by 195 · see citing works

HIV-1 Vpr function is mediated by interaction with the damage-specific DNA-binding protein DDB1

Schröfelbauer, B., Hakata, Y., & Landau, N. R. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0610167104 · Cited by 187 · see citing works

Models and Theory

Walsh, V. C. (1987) · The New Palgrave Dictionary of Economics · doi:10.1057/978-1-349-95121-5_923-1 · Cited by 184 · see citing works

Excision of cytosine and thymine from DNA by mutants of human uracil‐DNA glycosylase.

Kavli, B., Slupphaug, G., Mol, C. D., Arvai, A. S., Peterson, S. B., Tainer, J. A., & Krokan, H. E. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00710.x · Cited by 179 · see citing works

The novel DNA glycosylase, NEIL1, protects mammalian cells from radiation-mediated cell death

Rosenquist, T. A., Zaika, E. I., Fernandes, A. S., Zharkov, D. O., Miller, H., & Grollman, A. P. (2003) · DNA repair · doi:10.1016/s1568-7864(03)00025-9 · Cited by 179 · see citing works

Structural analysis of an Escherichia coli endonuclease VIII covalent reaction intermediate

Zharkov, D. O., Golan, G., Gilboa, R., Fernandes, A. S., Gerchman, S. E., Kycia, J. H., Rieger, R. A., Grollman, A. P., & Shoham, G. (2002) · The EMBO Journal · doi:10.1093/emboj/21.4.789 · Cited by 178 · see citing works

Mbd4 inactivation increases C→T transition mutations and promotes gastrointestinal tumor formation

Wong, E., Yang, K., Kuraguchi, M., Werling, U., Avdievich, E., Fan, K., Fazzari, M. J., Jin, B., Brown, A. M. C., Lipkin, M., et al. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.232579299 · Cited by 178 · see citing works

Product-assisted catalysis in base-excision DNA repair

Fromme, J. C., Bruner, S. D., Yang, W. Y., Karplus, M., & Verdine, G. L. (2003) · Nature Structural & Molecular Biology · doi:10.1038/nsb902 · Cited by 176 · see citing works

Detection of Damaged DNA Bases by DNA Glycosylase Enzymes

Friedman, J. I., & Stivers, J. T. (2010) · Biochemistry · doi:10.1021/bi100593a · Cited by 175 · see citing works

The critical active-site amine of the human 8-oxoguanine DNA glycosylase, hOgg1: direct identification, ablation and chemical reconstitution

Nash, H. M., Lu, R., Lane, W. S., & Verdinel, G. L. (1997) · Chemistry & Biology · doi:10.1016/s1074-5521(97)90225-8 · Cited by 172 · see citing works

5-Methylcytosine DNA glycosylase activity is also present in the human MBD4 (G/T mismatch glycosylase) and in a related avian sequence

Zhu, B. M. (2000) · Nucleic Acids Research · doi:10.1093/nar/28.21.4157 · Cited by 172 · see citing works

An endonuclease from Escherichia coli that introduces single polynucleotide chain scissions in ultraviolet-irradiated DNA.

Radman, M. (1976) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)33759-6 · Cited by 170 · see citing works

Isolation and Characterization of Endonuclease VIII from Escherichia coli

Melamede, R. J., Hatahet, Z., Kow, Y. W., Ide, H., & Wallace, S. S. (1994) · Biochemistry · doi:10.1021/bi00171a028 · Cited by 168 · see citing works

Functionality of Human Thymine DNA Glycosylase Requires SUMO-Regulated Changes in Protein Conformation

Steinacher, R., & Schär, P. (2005) · Current Biology · doi:10.1016/j.cub.2005.02.054 · Cited by 161 · see citing works

Accumulation of the Oxidative Base Lesion 8-Hydroxyguanine in DNA of Tumor-Prone Mice Defective in Both the Myh and Ogg1 DNA Glycosylases

Russo, M. T., Luca, G. D., Degan, P., Parlanti, E., Eugenia Dogliotti, Y., Barnes, D. E., Lindahl, T. L., Yang, H., Miller, J. H., & Bignami, M. (2004) · Cancer Research · doi:10.1158/0008-5472.can-04-0355 · Cited by 160 · see citing works

AID Targeting in Antibody Diversity

Pavri, R., & Nussenzweig, M. C. (2011) · Advances in immunology · doi:10.1016/b978-0-12-387663-8.00005-3 · Cited by 156 · see citing works

Escherichia coli mutY gene product is required for specific A-G----C.G mismatch correction.

Au, K. G., Cabrera, M., Miller, J. H., & Modrich, P. L. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.23.9163 · Cited by 153 · see citing works

Definitive Identification of Mammalian 5-Hydroxymethyluracil DNA N-Glycosylase Activity as SMUG1

Boorstein, R. J., Cummings, A., Marenstein, D. R., Chan, M. K., Ma, Y., Neubert, T. A., Brown, S. M., & Teebor, G. W. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106953200 · Cited by 152 · see citing works

Gene-targeted mice lacking the Ung uracil-DNA glycosylase develop B-cell lymphomas

Nilsen, H. L., Stamp, G., Andersen, S. B., Hrivnak, G., Krokan, H. E., Lindahl, T. L., & Barnes, D. E. (2003) · Oncogene · doi:10.1038/sj.onc.1206860 · Cited by 152 · see citing works

The versatile thymine DNA-glycosylase: a comparative characterization of the human, Drosophila and fission yeast orthologs

Hardeland, U. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg344 · Cited by 149 · see citing works

Studies on the Catalytic Mechanism of Five DNA Glycosylases

Sun, B., Latham, K. A., Dodson, M. L., & Lloyd, R. S. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.33.19501 · Cited by 148 · see citing works

5-Methylcytosine-DNA glycosylase activity is present in a cloned G/T mismatch DNA glycosylase associated with the chicken embryo DNA demethylation complex

Zhu, B., Zheng, Y., Heß, D., Angliker, H., Schwarz, S., Siegmann, M., Thiry, S., & Jost, J. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.100107597 · Cited by 145 · see citing works

Kinetics of the Action of Thymine DNA Glycosylase

Waters, T. R., & SWANN, P. F. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.32.20007 · Cited by 144 · see citing works

Structure and Specificity of the Vertebrate Anti-Mutator Uracil-DNA Glycosylase SMUG1

Wibley, J., Waters, T. R., Haushalter, K. A., Verdine, G. L., & Pearl, L. H. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00235-1 · Cited by 143 · see citing works

Xeroderma pigmentosum group C protein interacts physically and functionally with thymine DNA glycosylase

Shimizu, Y., Iwai, S., Hanaoka, F., & Sugasawa, K. (2002) · The EMBO Journal · doi:10.1093/emboj/cdg016 · Cited by 142 · see citing works

The α/β fold uracil DNA glycosylases: a common origin with diverse fates

Aravind, L., & Koonin, E. V. (2000) · Genome biology · doi:10.1186/gb-2000-1-4-research0007 · Cited by 141 · see citing works

Targeted deletion of alkylpurine-DNA-N-glycosylase in mice eliminates repair of 1, N 6 -ethenoadenine and hypoxanthine but not of 3, N 4 -ethenocytosine or 8-oxoguanine

Hang, B., Singer, B. A., Margison, G. P., & Elder, R. H. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.24.12869 · Cited by 140 · see citing works

Cell cycle‐specific UNG2 phosphorylations regulate protein turnover, activity and association with RPA

Hagen, L., Kavli, B., de Sousa, M. M. L., Torseth, K., Liabakk, N., Sundheim, O., Peña-Dı́az, J., Otterlei, M., Hørning, O. B., Jensen, O. N., et al. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601958 · Cited by 139 · see citing works

Purification and characterization of human 3-methyladenine-DNA glycosylase

Connor, T. R. O. (1993) · Nucleic Acids Research · doi:10.1093/nar/21.24.5561 · Cited by 137 · see citing works

Virion-associated Uracil DNA Glycosylase-2 and Apurinic/Apyrimidinic Endonuclease Are Involved in the Degradation of APOBEC3G-edited Nascent HIV-1 DNA

Yang, B., Chen, K., Zhang, C., Huang, S., & Zhang, H. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m606864200 · Cited by 135 · see citing works

Crystal structure of a thwarted mismatch glycosylase DNA repair complex

Barrett, T. E., Schärer, O. D., Savva, R., Brown, T., Jiricny, J., Verdine, G. L., & Pearl, L. H. (1999) · The EMBO Journal · doi:10.1093/emboj/18.23.6599 · Cited by 134 · see citing works

5-Fluorouracil Incorporated into DNA Is Excised by the Smug1 DNA Glycosylase to Reduce Drug Cytotoxicity

An, Q., Robins, P., Lindahl, T., & Barnes, D. E. (2007) · Cancer Research · doi:10.1158/0008-5472.can-06-2960 · Cited by 134 · see citing works

Retinoic Acid Receptors Interact Physically and Functionally with the T:G Mismatch-specific Thymine-DNA Glycosylase

Um, S., Harbers, M., Benecke, A., Pierrat, B., Losson, R., & Chambon, P. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.33.20728 · Cited by 134 · see citing works

Mechanisms of DNA Demethylation in Chicken Embryos

Jost, J., Siegmann, M., Sun, L., & Leung, R. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.17.9734 · Cited by 130 · see citing works

Separating Substrate Recognition from Base Hydrolysis in Human Thymine DNA Glycosylase by Mutational Analysis

Hardeland, U., Bentele, M., Jiricny, J., & Schär, P. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m005095200 · Cited by 130 · see citing works

The base excision repair enzyme MED1 mediates DNA damage response to antitumor drugs and is associated with mismatch repair system integrity

Cortellino, S., Turner, D. P., Masciullo, V., Schepis, F., Albino, D., Daniel, R., Skalka, A. M., Meropol, N. J., Alberti, C., Larue, L., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2334585100 · Cited by 127 · see citing works

UNG-initiated base excision repair is the major repair route for 5-fluorouracil in DNA, but 5-fluorouracil cytotoxicity depends mainly on RNA incorporation

Pettersen, H. S., Visnes, T., Vågbø, C. B., Svaasand, E. K., Doseth, B., Slupphaug, G., Kavli, B., & Krokan, H. E. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr563 · Cited by 125 · see citing works

Redox signaling between DNA repair proteins for efficient lesion detection

Boal, A. K., Genereux, J. C., Sontz, P. A., Gralnick, J. A., Newman, D. K., & Barton, J. K. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0908059106 · Cited by 124 · see citing works

Crystal structure of human thymine DNA glycosylase bound to DNA elucidates sequence-specific mismatch recognition

Maiti, A., Morgan, M. T., Pozharski, E. V., & Drohat, A. C. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0711061105 · Cited by 123 · see citing works

Envisioning the molecular choreography of DNA base excision repair

Parikh, S. S., Mol, C. D., Hosfield, D. J., & Tainer, J. A. (1999) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(99)80006-2 · Cited by 119 · see citing works

Base Excision by Thymine DNA Glycosylase Mediates DNA-Directed Cytotoxicity of 5-Fluorouracil

Kunz, C., Focke, F., Saito, Y., Schuermann, D., Lettieri, T., Selfridge, J., & Schär, P. (2009) · PLoS Biology · doi:10.1371/journal.pbio.1000091 · Cited by 112 · see citing works

Substrate specificity of the Ogg1 protein of Saccharomyces cerevisiae: excision of guanine lesions produced in DNA by ionizing radiation- or hydrogen peroxide/metal ion-generated free radicals

Karahalıl, B. (1998) · Nucleic Acids Research · doi:10.1093/nar/26.5.1228 · Cited by 112 · see citing works

Investigation of the substrate spectrum of the human mismatch‐specific DNA N ‐glycosylase MED1 (MBD4): Fundamental role of the catalytic domain

Petronzelli, F., Riccio, A., Markham, G. D., Seeholzer, S. H., Genuardi, M., Karbowski, M., Yeung, A. T., Matsumoto, Y., & Bellacosa, A. (2000) · Journal of Cellular Physiology · doi:10.1002/1097-4652(200012)185:3 · Cited by 110 · see citing works

Excision of Products of Oxidative DNA Base Damage by Human NTH1 Protein

Dizdaroğlu, M., Karahalıl, B., Sentürker, S., Buckley, T. J., & Roldán‐Arjona, T. (1998) · Biochemistry · doi:10.1021/bi9819071 · Cited by 110 · see citing works

A Substrate Recognition Role for the [4Fe-4S]2+ Cluster of the DNA Repair Glycosylase MutY

Porello, S. L., Cannon, M. J., & David, S. S. (1998) · Biochemistry · doi:10.1021/bi972433t · Cited by 108 · see citing works

C → T mutagenesis and γ‐radiation sensitivity due to deficiency in the Smug1 and Ung DNA glycosylases

An, Q., Robins, P., Lindahl, T. L., & Barnes, D. E. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600689 · Cited by 108 · see citing works

Isolation and structure of a cDNA expressing a mammalian 3‐methyladenine‐DNA glycosylase.

O'Connor, T. R., & Laval, F. (1990) · The EMBO Journal · doi:10.1002/j.1460-2075.1990.tb07534.x · Cited by 107 · see citing works

Targeted Deletion of mNth1 Reveals a Novel DNA Repair Enzyme Activity

Ocampo, M. A., Chaung, W., Marenstein, D. R., Chan, M. K., Altamirano, A. M., Basu, A. K., Boorstein, R. J., Cunningham, R. P., & Teebor, G. W. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.17.6111-6121.2002 · Cited by 104 · see citing works

An Evolutionary Analysis of the Helix-Hairpin-Helix Superfamily of DNA Repair Glycosylases

Denver, D. R. (2003) · Molecular Biology and Evolution · doi:10.1093/molbev/msg177 · Cited by 103 · see citing works

DNA Repair in Mammalian Cells

Kunz, C., Saito, Y., & Schär, P. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-8739-9 · Cited by 101 · see citing works

Recognition and Processing of a New Repertoire of DNA Substrates by Human 3-Methyladenine DNA Glycosylase (AAG)

Lee, C. I., Delaney, J. C., Kartalou, M., Lingaraju, G. M., Maor-Shoshani, A., Essigmann, J. M., & Samson, L. D. (2009) · Biochemistry · doi:10.1021/bi8018898 · Cited by 98 · see citing works

Cell cycle regulation as a mechanism for functional separation of the apparently redundant uracil DNA glycosylases TDG and UNG2

Hardeland, U., Kunz, C., Focke, F., Szadkowski, M., & Schär, P. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm337 · Cited by 95 · see citing works

5-hydroxymethylcytosine DNA glycosylase activity in mammalian tissue

Cannon, S. V., Cummings, A., & Teebor, G. W. (1988) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(88)80489-3 · Cited by 94 · see citing works

SMUG1 is able to excise uracil from immunoglobulin genes: insight into mutation versus repair

Noia, J. M. D., Rada, C. A., & Neuberger, M. S. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7600939 · Cited by 90 · see citing works

Aag-initiated base excision repair drives alkylation-induced retinal degeneration in mice

Meira, L. B., Moroski-Erkul, C. A., Green, S. L., Calvo, J. A., Bronson, R. T., Shah, D., & Samson, L. D. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0807030106 · Cited by 89 · see citing works

Counteracting the mutagenic effect of hydrolytic deamination of DNA 5‐methylcytosine residues at high temperature: DNA mismatch N‐glycosylase Mig.Mth of the thermophilic archaeon Methanobacterium thermoautotrophicum THF.

Horst, J. P., & Fritz, H. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00929.x · Cited by 83 · see citing works

Interference of mismatch and base excision repair during the processing of adjacent U/G mispairs may play a key role in somatic hypermutation

Schanz, S., Castor, D., Fischer, F., & Jiricny, J. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0901726106 · Cited by 81 · see citing works

Overexpression of 5-methylcytosine DNA glycosylase in human embryonic kidney cells EcR293 demethylates the promoter of a hormone-regulated reporter gene

Zhu, B., Benjamin, D., Zheng, Y., Angliker, H., Thiry, S., Siegmann, M., & Jost, J. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.091097298 · Cited by 78 · see citing works

Human Endonuclease III Acts Preferentially on DNA Damage Opposite Guanine Residues in DNA

Eide, L., Luna, L., Gustad, E. C., Henderson, P. T., Essigmann, J. M., Demple, B., & Seeberg, E. C. (2001) · Biochemistry · doi:10.1021/bi0028901 · Cited by 69 · see citing works

An unexpectedly high excision capacity for mispaired 5-hydroxymethyluracil in human cell extracts

Rusmintratip, V., & Sowers, L. C. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.26.14183 · Cited by 67 · see citing works

Hematopoietic Tissue–Specific Expression of Mouse Neil3 for Endonuclease VIII–Like Protein

Torisu, K., Tsuchimoto, D., Ohnishi, Y., & Nakabeppu, Y. (2005) · The Journal of Biochemistry · doi:10.1093/jb/mvi168 · Cited by 67 · see citing works

Both base excision repair and O-6-methylguanine-DNA methyltransferase protect against methylation-induced colon carcinogenesis

Samson, L. D., Wirtz, S. J., Nagel, G., Eshkind, L., Neurath, M. F., & Kaina, B. (2010) · DSpace@MIT (Massachusetts Institute of Technology) · Cited by 64 · see citing works

The association of polymorphisms in DNA base excision repair genes XRCC1, OGG1 and MUTYH with the risk of childhood acute lymphoblastic leukemia

Stańczyk, M. B., Śliwiński, T., Cuchra, M., Zubowska, M., Bielecka-Kowalska, A., Kowalski, M., Szemraj, J., Mlynarski, W. M., & Majsterek, I. (2010) · Molecular Biology Reports · doi:10.1007/s11033-010-0127-x · Cited by 61 · see citing works

Role of Two Strictly Conserved Residues in Nucleotide Flipping and N-Glycosylic Bond Cleavage by Human Thymine DNA Glycosylase

Maiti, A., Morgan, M. T., & Drohat, A. C. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.062356 · Cited by 56 · see citing works

Purification and Characterization of 5-Hydroxymethyluracil-DNA Glycosylase from Calf Thymus

Cannon‐Carlson, S., Gokhale, H., & Teebor, G. W. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)51629-x · Cited by 54 · see citing works

Escherichia coli Apurinic-Apyrimidinic Endonucleases Enhance the Turnover of the Adenine Glycosylase MutY with G:A Substrates

Pope, M. A., Porello, S. L., & David, S. S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203037200 · Cited by 53 · see citing works

8-Oxoguanine incision activity is impaired in lung tissues of NSCLC patients with the polymorphism of OGG1 and XRCC1 genes

Janik, J., Swoboda, M., Janowska, B., Cieśla, J., Gackowski, D., Kowalewski, J., Oliński, R., Tudek, B., & Speina, E. (2011) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2011.02.009 · Cited by 51 · see citing works

The RNA moiety of chick embryo 5-methylcytosine- DNA glycosylase targets DNA demethylation

Jost, J. P. (1997) · Nucleic Acids Research · doi:10.1093/nar/25.22.4545 · Cited by 51 · see citing works

The Concerted Action of Msh2 and UNG Stimulates Somatic Hypermutation at A · T Base Pairs

Frieder, D., Larijani, M., Collins, C., Shulman, M. J., & Martín, A. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00647-09 · Cited by 51 · see citing works

Nontarget DNA binding shapes the dynamic landscape for enzymatic recognition of DNA damage

Friedman, J. I., Majumdar, A. K., & Stivers, J. T. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp161 · Cited by 49 · see citing works

Requirement of Non-canonical Activity of Uracil DNA Glycosylase for Class Switch Recombination

Begum, N. A., Izumi, N., Nishikori, M., Nagaoka, H., Shinkura, R., & Honjo, T. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m607439200 · Cited by 47 · see citing works

Further evidence for involvement of a noncanonical function of uracil DNA glycosylase in class switch recombination

Begum, N. A., Stanlie, A., Doi, T., Sasaki, Y., Jin, H. W., Kim, Y. S., Nagaoka, H., & Honjo, T. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0813252106 · Cited by 43 · see citing works

Cutting Edge: The G-U Mismatch Glycosylase Methyl-CpG Binding Domain 4 Is Dispensable for Somatic Hypermutation and Class Switch Recombination

Bardwell, P. D., Martín, A., Wong, E., Li, Z., Edelmann, W., & Scharff, M. D. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.170.4.1620 · Cited by 43 · see citing works

Increased spontaneous mutation frequency in human cells expressing the phage PBS2-encoded inhibitor of uracil-DNA glycosylase

Radany, E. H., Dornfeld, K. J., Sanderson, R. J., Savage, M. K., Majumdar, A., Seidman, M. M., & Mosbaugh, D. W. (2000) · Mutation Research/DNA Repair · doi:10.1016/s0921-8777(00)00040-9 · Cited by 41 · see citing works

A new member of the endonuclease III family of DNA repair enzymes that removes methylated purines from DNA

Begley, T. J., Haas, B. J., Noel, J., Shekhtman, A. G., Williams, W. A., & Cunningham, R. P. (1999) · Current Biology · doi:10.1016/s0960-9822(99)80288-7 · Cited by 37 · see citing works

Stimulation of DNA Glycosylase Activities by XPC Protein Complex: Roles of Protein‐Protein Interactions

Shimizu, Y., Uchimura, Y., Dohmae, N., Saitoh, H., Hanaoka, F., & Sugasawa, K. (2010) · Journal of Nucleic Acids · doi:10.4061/2010/805698 · Cited by 33 · see citing works

A CpG-rich RNA and an RNA helicase tightly associated with the DNA demethylation complex are present mainly in dividing chick embryo cells

Schwarz, S., Bourgeois, C. A., Soussaline, F. P., Homsy, C., Podestà, A., & Jost, J. (2000) · European Journal of Cell Biology · doi:10.1078/0171-9335-00070 · Cited by 12 · see citing works

Both base excision repair and O6-methylguanine-DNA methyltransferase protect against methylation-induced colon carcinogenesis

Wirtz, S. J., Nagel, G., Eshkind, L. G., et al. (2010) · Carcinogenesis · doi:10.1093/carcin/bgq174 · Cited by 2 · 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

Base Excision Repair

Krokan, H. E., & Bjoras, M. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a012583 · Cited by 1,322 · see citing works

Inflammation-induced DNA damage, mutations and cancer

Kay, J. E., Thadhani, E., Samson, L. D., & Engelward, B. P. (2019) · DNA repair · doi:10.1016/j.dnarep.2019.102673 · Cited by 481 · 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

Mammalian Base Excision Repair: the Forgotten Archangel

Dianov, G. L., & Hübscher, U. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt076 · Cited by 381 · see citing works

DNA Damage/Repair Management in Cancers

Alhmoud, J. F., Woolley, J. F., Moustafa, A. A., & Malki, M. I. (2020) · Cancers · doi:10.3390/cancers12041050 · Cited by 378 · see citing works

DNA Methylation, Its Mediators and Genome Integrity

Meng, H., Cao, Y., Qin, J., Song, X., Zhang, Q., Shi, Y. S., & Cao, L. (2015) · International Journal of Biological Sciences · doi:10.7150/ijbs.11218 · Cited by 327 · see citing works

Elucidating the mechanisms of Temozolomide resistance in gliomas and the strategies to overcome the resistance.

Tomar, M. S., Kumar, A., Srivastava, C., & Shrivastava, A. (2021) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2021.188616 · Cited by 328 · see citing works

Tet oxidizes thymine to 5-hydroxymethyluracil in mouse embryonic stem cell DNA

Pfaffeneder, T., Spada, F., Wagner, M., Brandmayr, C., Laube, S. K., Eisen, D., Truß, M., Steinbacher, J., Hackner, B., Kotljarova, O., et al. (2014) · Nature Chemical Biology · doi:10.1038/nchembio.1532 · Cited by 306 · see citing works

Coordination of DNA single strand break repair

Abbotts, R., & Wilson, D. M. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.11.039 · Cited by 240 · see citing works

Biochemical reconstitution of TET1–TDG–BER-dependent active DNA demethylation reveals a highly coordinated mechanism

Weber, A. R., Krawczyk, C., Robertson, A. B., Kuśnierczyk, A., Vågbø, C. B., Schuermann, D., Klungland, A., & Schär, P. (2016) · Nature Communications · doi:10.1038/ncomms10806 · Cited by 233 · see citing works

Base excision repair of oxidative DNA damage from mechanism to disease

Freudenthal, B. (2017) · Frontiers in bioscience · doi:10.2741/4555 · Cited by 230 · see citing works

Biological Aspects in Food Preservation by Ultraviolet Light: a Review

Gayán, E., Condón, S., & Álvarez, I. (2013) · Food and Bioprocess Technology · doi:10.1007/s11947-013-1168-7 · Cited by 228 · see citing works

HDAC1 modulates OGG1-initiated oxidative DNA damage repair in the aging brain and Alzheimer’s disease

Pao, P.-C., Patnaik, D., Watson, L. A., Gao, F., Pan, L., Wang, J., Adaikkan, C., Penney, J., Cam, H. P., Huang, W.-C., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-16361-y · Cited by 216 · 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

DNA repair mechanisms and their clinical impact in glioblastoma

Erasimus, H., Gobin, M., Niclou, S. P., & Dyck, E. V. (2016) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2016.05.005 · Cited by 189 · see citing works

Recent advances in the structural mechanisms of DNA glycosylases

Brooks, S. C., Adhikary, S., Rubinson, E. H., & Eichman, B. F. (2012) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2012.10.005 · Cited by 178 · see citing works

The Mitochondrial Response to DNA Damage

Rong, Z., Tu, P., Xu, P., Sun, Y., Yu, F., Tu, N., Guo, L., & Yang, Y. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.669379 · Cited by 177 · see citing works

Focus on UV-Induced DNA Damage and Repair—Disease Relevance and Protective Strategies

Kciuk, M., Marciniak, B., Mojzych, M., & Kontek, R. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21197264 · Cited by 168 · see citing works

DNA Damage Response in Cancer Therapy and Resistance: Challenges and Opportunities

Jurkovičová, D., Neophytou, C. M., Gašparović, A. Č., & Gonçalves, A. C. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232314672 · Cited by 170 · see citing works

Impact of oxidative stress on telomere biology

Ahmed, W., & Lingner, J. (2018) · Differentiation · doi:10.1016/j.diff.2017.12.002 · Cited by 153 · see citing works

DNA damage related crosstalk between the nucleus and mitochondria

Saki, M. R., & Prakash, A. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.11.050 · Cited by 151 · see citing works

SOG1 activator and MYB3R repressors regulate a complex DNA damage network in Arabidopsis

Bourbousse, C., Vegesna, N., & Law, J. A. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1810582115 · Cited by 152 · see citing works

The roles of microphthalmia-associated transcription factor and pigmentation in melanoma

Hsiao, J. J., & Fisher, D. E. (2014) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2014.07.019 · Cited by 148 · see citing works

Base Excision Repair in the Mitochondria

Prakash, A., & Doublié, S. (2015) · Journal of Cellular Biochemistry · doi:10.1002/jcb.25103 · Cited by 147 · see citing works

Base Excision Repair, a Pathway Regulated by Posttranslational Modifications

Carter, R. J., & Parsons, J. L. (2016) · Molecular and Cellular Biology · doi:10.1128/mcb.00030-16 · Cited by 147 · see citing works

Insights into the Pathogenesis of Neurodegenerative Diseases: Focus on Mitochondrial Dysfunction and Oxidative Stress

Jurcău, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222111847 · Cited by 150 · see citing works

Altering DNA Repair to Improve Radiation Therapy: Specific and Multiple Pathway Targeting

Biau, J., Chautard, E., Verrelle, P., & Dutreix, M. (2019) · Frontiers in Oncology · doi:10.3389/fonc.2019.01009 · Cited by 137 · see citing works

5-Methylcytosine DNA Demethylation: More Than Losing a Methyl Group

Franchini, D., Schmitz, K.-M., & Petersen‐Mahrt, S. K. (2012) · Annual Review of Genetics · doi:10.1146/annurev-genet-110711-155451 · Cited by 128 · see citing works

Complex DNA repair pathways as possible therapeutic targets to overcome temozolomide resistance in glioblastoma

Yoshimoto, K., Mizoguchi, M., Hata, N., Murata, H., Hatae, R., Amano, T., Nakamizo, A., & Sasaki, T. (2012) · Frontiers in Oncology · doi:10.3389/fonc.2012.00186 · Cited by 126 · see citing works

Base excision repair and its implications to cancer therapy

Grundy, G. J., & Parsons, J. L. (2020) · Essays in Biochemistry · doi:10.1042/ebc20200013 · Cited by 121 · see citing works

TET Enzymes in the Immune System: From DNA Demethylation to Immunotherapy, Inflammation, and Cancer

López-Moyado, I. F., Ko, M., Hogan, P. G., & Rao, A. (2024) · Annual Review of Immunology · doi:10.1146/annurev-immunol-080223-044610 · Cited by 116 · see citing works

DNA Repair Pathways and Mechanisms

Dexheimer, T. S. (2012) · Springer eBooks · doi:10.1007/978-94-007-4590-2_2 · Cited by 116 · see citing works

Protective effects of Manuka honey on LPS-treated RAW 264.7 macrophages. Part 2: Control of oxidative stress induced damage, increase of antioxidant enzyme activities and attenuation of inflammation

Gasparrini, M., Afrin, S., Forbes-Hernández, T. Y., Cianciosi, D., Reboredo‐Rodríguez, P., Amici, A., Battino, M. A., & Giampieri, F. (2018) · Food and Chemical Toxicology · doi:10.1016/j.fct.2018.08.001 · Cited by 118 · see citing works

Genotoxic therapy and resistance mechanism in gliomas

Lang, F., Liu, Y., Chou, F.-J., & Yang, C. (2021) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2021.107922 · Cited by 113 · see citing works

Protecting DNA from errors and damage: an overview of DNA repair mechanisms in plants compared to mammals

Spampinato, C. P. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2436-2 · Cited by 110 · see citing works

Mutating for Good: DNA Damage Responses During Somatic Hypermutation

Pilzecker, B., & Jacobs, H. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.00438 · Cited by 108 · see citing works

The interaction between cytosine methylation and processes of DNA replication and repair shape the mutational landscape of cancer genomes

Poulos, R. C., Olivier, J., & Wong, J. W. H. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx463 · Cited by 93 · see citing works

Mammalian DNA base excision repair: Dancing in the moonlight

Caldecott, K. W. (2020) · DNA repair · doi:10.1016/j.dnarep.2020.102921 · Cited by 101 · see citing works

TET-mediated oxidation of methylcytosine causes TDG or NEIL glycosylase dependent gene reactivation

Müller, U., Bauer, C., Siegl, M., Rottach, A., & Leonhardt, H. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku552 · Cited by 97 · see citing works

Repair of naturally occurring mismatches can induce mutations in flanking DNA

Chen, J., Miller, B., & Furano, A. V. (2014) · eLife · doi:10.7554/elife.02001 · Cited by 95 · see citing works

ATM prevents DSB formation by coordinating SSB repair and cell cycle progression

Khoronenkova, S. V., & Dianov, G. L. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1416031112 · Cited by 98 · see citing works

Gadd45a promotes DNA demethylation through TDG

Li, Z., Gu, T., Weber, A. R., Shen, J., Li, B.-Z., Xie, Z., Yin, R., Guo, F., Liu, X., Tang, F., et al. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv283 · Cited by 95 · see citing works

The fate of damaged mitochondrial DNA in the cell

Liao, S., Chen, L., Song, Z., & He, H. (2022) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2022.119233 · Cited by 90 · see citing works

DNA Base Excision Repair in Plants: An Unfolding Story With Familiar and Novel Characters

Roldán‐Arjona, T., Ariza, R. R., & Córdoba‐Cañero, D. (2019) · Frontiers in Plant Science · doi:10.3389/fpls.2019.01055 · Cited by 88 · see citing works

Epigenetic Regulation During Plant Development and the Capacity for Epigenetic Memory

Hemenway, E. A., & Gehring, M. A. (2023) · Annual Review of Plant Biology · doi:10.1146/annurev-arplant-070122-025047 · Cited by 86 · see citing works

Active DNA demethylation by DNA repair: Facts and uncertainties

Schuermann, D., Weber, A. R., & Schär, P. (2016) · DNA repair · doi:10.1016/j.dnarep.2016.05.013 · Cited by 82 · see citing works

Programmable deaminase-free base editors for G-to-Y conversion by engineered glycosylase

Tong, H., Liu, N., Wei, Y., Zhou, Y., Li, Y., Wu, D., Jin, M., Cui, S., Li, H., Li, G., et al. (2023) · National Science Review · doi:10.1093/nsr/nwad143 · Cited by 85 · see citing works

DNA Damage and Repair in Schizophrenia and Autism: Implications for Cancer Comorbidity and Beyond

Markkanen, E., Meyer, U., & Dianov, G. L. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17060856 · Cited by 84 · see citing works

Sequencing abasic sites in DNA at single-nucleotide resolution

Liu, Z. J., Martínez Cuesta, S., van Delft, P., & Balasubramanian, S. (2019) · Nature Chemistry · doi:10.1038/s41557-019-0279-9 · Cited by 83 · see citing works

Mitochondrial quality control in health and cardiovascular diseases

Atici, A. E., Crother, T. R., & Rivas, M. N. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1290046 · Cited by 83 · see citing works

PRDX1 and MTH1 cooperate to prevent ROS-mediated inhibition of telomerasePreprint

Ahmed, W., & Lingner, J. (2018) · Genes & Development · doi:10.1101/gad.313460.118 · Cited by 78 · see citing works

MUTYH DNA glycosylase: the rationale for removing undamaged bases from the DNA

Markkanen, E., Dorn, J., & Hübscher, U. (2013) · Frontiers in Genetics · doi:10.3389/fgene.2013.00018 · Cited by 77 · see citing works

The Response to Oxidative DNA Damage in Neurons: Mechanisms and Disease

Narciso, L., Parlanti, E., Racaniello, M., Simonelli, V., Cardinale, A., Merlo, D., & Dogliotti, E. (2016) · Neural Plasticity · doi:10.1155/2016/3619274 · Cited by 75 · see citing works

Base-Excision-Repair-Induced Construction of a Single Quantum-Dot-Based Sensor for Sensitive Detection of DNA Glycosylase Activity

Wang, L., Ma, F., Tang, B., & Zhang, C. (2016) · Analytical Chemistry · doi:10.1021/acs.analchem.6b00664 · Cited by 74 · see citing works

Targeting BER enzymes in cancer therapy

Visnes, T., Grube, M., Hanna, B., Benitéz‐Buelga, C., Cázares‐Körner, A., & Helleday, T. (2018) · DNA repair · doi:10.1016/j.dnarep.2018.08.015 · Cited by 74 · see citing works

Oxidatively generated base modifications in DNA: Not only carcinogenic risk factor but also regulatory mark?

Seifermann, M., & Epe, B. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.11.018 · Cited by 71 · see citing works

Error-free versus mutagenic processing of genomic uracil—Relevance to cancer

Krokan, H. E., Sætrom, P., Aas, P. A., Pettersen, H. S., Kavli, B., & Slupphaug, G. (2014) · DNA repair · doi:10.1016/j.dnarep.2014.03.028 · Cited by 66 · see citing works

Living Organisms Author Their Read-Write Genomes in Evolution

Shapiro, J. A. (2017) · Biology · doi:10.3390/biology6040042 · Cited by 68 · see citing works

Temozolomide and Pituitary Tumors: Current Understanding, Unresolved Issues, and Future Directions

Syro, L. V., Rotondo, F., Camargo, M., Ortiz, L. D., Serna, C. A., & Kovács, K. (2018) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00318 · Cited by 68 · see citing works

The Relevance of G-Quadruplexes for DNA Repair

Linke, R., Limmer, M., Juranek, S., Heine, A., & Paeschke, K. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222212599 · Cited by 64 · see citing works

DNA repair as a shared hallmark in cancer and ageing

Clarke, T. L., & Mostoslavsky, R. (2022) · Molecular Oncology · doi:10.1002/1878-0261.13285 · Cited by 68 · see citing works

Mitochondrial DNA Repair in Neurodegenerative Diseases and Ageing

Bazzani, V., Redin, M. E., McHale, J., Perrone, L., & Vascotto, C. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231911391 · Cited by 66 · see citing works

Facilitated Diffusion Mechanisms in DNA Base Excision Repair and Transcriptional Activation

Esadze, A., & Stivers, J. T. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00513 · Cited by 64 · see citing works

The radiobiology of HPV-positive and HPV-negative head and neck squamous cell carcinoma

Zhou, C., & Parsons, J. L. (2020) · Expert Reviews in Molecular Medicine · doi:10.1017/erm.2020.4 · Cited by 63 · see citing works

Differential effects of silver nanoparticles on DNA damage and DNA repair gene expression in Ogg1-deficient and wild type mice

Nallanthighal, S., Chan, C., Murray, T. M., Mosier, A. P., Cady, N. C., & Reliene, R. (2017) · Nanotoxicology · doi:10.1080/17435390.2017.1388863 · Cited by 63 · see citing works

Resolving DNA Damage: Epigenetic Regulation of DNA Repair

Karakaidos, P., Karagiannis, D., & Rampias, T. N. (2020) · Molecules · doi:10.3390/molecules25112496 · Cited by 61 · see citing works

Tackling PARP inhibitor resistance

Fugger, K., Hewitt, G., West, S. C., & Boulton, S. J. (2021) · Trends in cancer · doi:10.1016/j.trecan.2021.08.007 · Cited by 62 · see citing works

5-Formyl- and 5-Carboxydeoxycytidines Do Not Cause Accumulation of Harmful Repair Intermediates in Stem Cells

Rahimoff, R., Kosmatchev, O., Kirchner, A., Pfaffeneder, T., Spada, F., Brantl, V., Müller, M., & Carell, T. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b04131 · Cited by 62 · see citing works

Delivery Approaches for Therapeutic Genome Editing and Challenges

Ates, I., Rathbone, T., Stuart, C., Bridges, P. H., & Cottle, R. N. (2020) · Genes · doi:10.3390/genes11101113 · Cited by 60 · see citing works

Modification mapping by nanopore sequencing

White, L. K., & Hesselberth, J. R. (2022) · Frontiers in Genetics · doi:10.3389/fgene.2022.1037134 · Cited by 58 · see citing works

Genome-wide mapping of 5-hydroxymethyluracil in the eukaryote parasite Leishmania

Kawasaki, F., Beraldi, D., Hardisty, R. E., McInroy, G. R., van Delft, P., & Balasubramanian, S. (2017) · Genome biology · doi:10.1186/s13059-017-1150-1 · Cited by 59 · see citing works

An insight into the mechanisms of homeostasis in extremophiles

Somayaji, A., Dhanjal, C. R., Lingamsetty, R., Vinayagam, R., Selvaraj, R., Varadavenkatesan, T., & Govarthanan, M. (2022) · Microbiological Research · doi:10.1016/j.micres.2022.127115 · Cited by 59 · see citing works

A short review on the implications of base excision repair pathway for neurons: Relevance to neurodegenerative diseases

Mantha, A. K., Sarkar, B., & Tell, G. (2013) · Mitochondrion · doi:10.1016/j.mito.2013.10.007 · Cited by 58 · see citing works

Biological Functions of Hydrogen Sulfide in Plants

Yang, Z., Wang, X., Feng, J., & Zhu, S. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232315107 · Cited by 56 · see citing works

A Decade of Biochemical and Structural Studies of the DNA Repair Machinery of Deinococcus radiodurans : Major Findings, Functional and Mechanistic Insight and Challenges

Timmins, J., & Moe, E. (2016) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2016.04.001 · Cited by 57 · 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

Ultrafast Oxime Formation Enables Efficient Fluorescence Light-up Measurement of DNA Base Excision

Wilson, D. L., & Kool, E. T. (2019) · Journal of the American Chemical Society · doi:10.1021/jacs.9b09812 · Cited by 54 · see citing works

Role of Oxidative DNA Damage and Repair in Atrial Fibrillation and Ischemic Heart Disease

Hu, L., Wang, Z., Carmone, C., Keijer, J., & Zhang, D. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22083838 · Cited by 51 · see citing works

Regulation of oxidative DNA damage repair: The adenine:8-oxo-guanine problem

Markkanen, E., Hübscher, U., & van Loon, B. (2012) · Cell Cycle · doi:10.4161/cc.11.6.19448 · Cited by 50 · see citing works

DNA damage and repair following traumatic brain injury

Davis, C. K., & Vemuganti, R. (2020) · Neurobiology of Disease · doi:10.1016/j.nbd.2020.105143 · Cited by 49 · see citing works

AOP report: Development of an adverse outcome pathway for oxidative DNA damage leading to mutations and chromosomal aberrations

Cho, E., Allemang, A., Audebert, M., Chauhan, V., Dertinger, S. D., Hendriks, G., Luijten, M., Marchetti, F., Minocherhomji, S., Pfuhler, S., et al. (2022) · Environmental and Molecular Mutagenesis · doi:10.1002/em.22479 · Cited by 48 · see citing works

The inhibitory effect of Manuka honey on human colon cancer HCT-116 and LoVo cell growth. Part 2: Induction of oxidative stress, alteration of mitochondrial respiration and glycolysis, and suppression of metastatic ability

Afrin, S., Giampieri, F., Gasparrini, M., Forbes-Hernández, T. Y., Cianciosi, D., Reboredo‐Rodríguez, P., Manna, P. P., Zhang, J., Quiles, J. L., & Battino, M. A. (2018) · Food & Function · doi:10.1039/c8fo00165k · Cited by 49 · see citing works

ADP‐ribosylation of histone variant H2AX promotes base excision repair

Chen, Q., Bian, C., Wang, X., Liu, X., Kassab, M. A., Yu, Y., & Yu, X. (2020) · The EMBO Journal · doi:10.15252/embj.2020104542 · Cited by 46 · see citing works

Regular exercise participation improves genomic stability in diabetic patients: an exploratory study to analyse telomere length and DNA damage

Dimauro, I., Sgura, A., Pittaluga, M., Magi, F., Fantini, C., Mancinelli, R., Sgadari, A., Fulle, S., & Caporossi, D. (2017) · Scientific Reports · doi:10.1038/s41598-017-04448-4 · Cited by 47 · see citing works

Conformational Dynamics of DNA Repair by Escherichia coli Endonuclease III

Kuznetsov, N. A., Kladova, O. A., Кузнецова, А. А., Ishchenko, A. A., Saparbaev, M. K., Zharkov, D. O., & Fedorova, O. S. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.621128 · Cited by 44 · see citing works

Assessment of DNA Epigenetic Modifications

Yuan, B. (2019) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.9b00372 · Cited by 45 · see citing works

When DNA repair goes wrong: BER-generated DNA-protein crosslinks to oxidative lesions

Quiñones, J. L., & Demple, B. (2016) · DNA repair · doi:10.1016/j.dnarep.2016.05.014 · Cited by 43 · see citing works

The Biochemical Role of the Human NEIL1 and NEIL3 DNA Glycosylases on Model DNA Replication Forks

Albelazi, M. S., Martin, P. R., Mohammed, S., Mutti, L., Parsons, J. L., & Elder, R. H. (2019) · Genes · doi:10.3390/genes10040315 · Cited by 43 · see citing works

A combined Far-FTIR, FTIR Spectromicroscopy, and DFT Study of the Effect of DNA Binding on the [4Fe4S] Cluster Site in EndoIII

Hassan, A., Macedo, L. J. A., de Souza, J. C. P., Lima, F. C. D. A., & Crespilho, F. N. (2020) · Scientific Reports · doi:10.1038/s41598-020-58531-4 · Cited by 42 · see citing works

Rapid inactivation and proteasome-mediated degradation of OGG1 contribute to the synergistic effect of hyperthermia on genotoxic treatments

Fantini, D., Moritz, E., Auvré, F., Amouroux, R., Campalans, A., Epe, B., Bravard, A., & Radicella, J. P. (2013) · DNA repair · doi:10.1016/j.dnarep.2012.12.006 · Cited by 42 · see citing works

Cisplatin in the era of PARP inhibitors and immunotherapy

Duan, M., Leng, S., & Mao, P. (2024) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2024.108642 · Cited by 43 · see citing works

Role of DNA repair in host immune response and inflammation

Fontes-Dantas, F. L., Pinheiro, D. M. L., de Oliveira, A. H. S., Oliveira, R. K. D. M., Lajus, T. B. P., & Agnez‐Lima, L. F. (2014) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2014.11.004 · Cited by 41 · see citing works

SUMOylation coordinates BERosome assembly in active DNA demethylation during cell differentiation

Steinacher, R., Barekati, Z., Botev, P., Kuśnierczyk, A., Slupphaug, G., & Schär, P. (2018) · The EMBO Journal · doi:10.15252/embj.201899242 · Cited by 41 · see citing works

Genes, Gender, Environment, and Novel Functions of Estrogen Receptor Beta in the Susceptibility to Neurodevelopmental Disorders

Varshney, M., & Nalvarte, I. (2017) · Brain Sciences · doi:10.3390/brainsci7030024 · Cited by 40 · see citing works

DNA Damage/Repair Management in Cancers

Alhmoud, J. F., Woolley, J. F., Moustafa, A. A., & Mallei, M. I. (2021) · doi:10.1201/9781003180449-12 · Cited by 38 · see citing works

Self‐Resistance to an Antitumor Antibiotic: A DNA Glycosylase Triggers the Base‐Excision Repair System in Yatakemycin Biosynthesis

Xu, H., Huang, W. S., He, Q., Zhao, Z., Zhang, F., Wang, R., Kang, J., & Tang, G. (2012) · Angewandte Chemie International Edition · doi:10.1002/anie.201204109 · Cited by 39 · see citing works

The role of the N-terminal domain of human apurinic/apyrimidinic endonuclease 1, APE1, in DNA glycosylase stimulation

Kladova, O. A., Bażlekowa, M., Baconnais, S., Piétrement, O., Ishchenko, A. A., Matkarimov, B. T., Iakovlev, D. A., Vasenko, A. S., Fedorova, O. S., Cam, É. L., et al. (2018) · DNA repair · doi:10.1016/j.dnarep.2018.02.001 · Cited by 39 · see citing works

NEIL1 and NEIL2 DNA glycosylases protect neural crest development against mitochondrial oxidative stress

Han, D., Schomacher, L., Schüle, K. M., Mallick, M., Musheev, M. U., Karaulanov, E., Krebs, L., von Seggern, A., & Niehrs, C. (2019) · eLife · doi:10.7554/elife.49044 · Cited by 38 · see citing works

Alkyladenine DNA glycosylase associates with transcription elongation to coordinate DNA repair with gene expression

Montaldo, N. P., Bordin, D. L., Brambilla, A., Rösinger, M., Martin, S. L. F., Bjørås, K. Ø., Bradamante, S., Aas, P. A., Furrer, A., Olsen, L. C., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-13394-w · Cited by 39 · see citing works

Communicated by: E. Nigg

Jacobs, A. L., & Schär, P. (2013)

DNA Glycosylases: Mechanisms

Drohat, A. C., & Maiti, A. (2013) · Encyclopedia of Biological Chemistry · doi:10.1016/b978-0-12-378630-2.00279-6 · Cited by 3 · see citing works

DNA repair | DNA Glycosylases

Drohat, A. C. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-819460-7.00256-5 · Cited by 1 · see citing works

Emerging Roles of DNA Glycosylases and the Base Excision Repair Pathway

Mullins, E. A., Rodriguez, A. A., Bradley, N. P., & Eichman, B. F. (2019) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2019.04.006 · Cited by 114 · see citing works

Recent advances in the structural mechanisms of DNA glycosylases

Brooks, S. C., Adhikary, S., Rubinson, E. H., & Eichman, B. F. (2012) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2012.10.005 · Cited by 178 · see citing works