Base excision repair: A critical player in many games

Wallace, Susan S.

doi:10.1016/j.dnarep.2014.03.030

Cited by 401DNA Repair MechanismsDNA and Nucleic Acid ChemistryEpigenetics and DNA Methylation

Base excision repair: A critical player in many games

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Wallace, Susan S.·2014·DNA Repair

DOI 10.1016/j.dnarep.2014.03.030PMC PMC4100245

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Abstract

This perspective reviews the many dimensions of base excision repair from a 10,000 foot vantage point and provides one person's view on where the field is headed. Enzyme function is considered under the lens of X-ray diffraction and single molecule studies. Base excision repair in chromatin and telomeres, regulation of expression and the role of posttranslational modifications are also discussed in the context of enzyme activities, cellular localization and interacting partners. The specialized roles that base excision repair play in transcriptional activation by active demethylation and targeted oxidation as well as how base excision repair functions in the immune processes of somatic hypermutation and class switch recombination and its possible involvement in retroviral infection are also discussed. Finally the complexities of oxidative damage and its repair and its link to neurodegenerative disorders, as well as the role of base excision repair as a tumor suppressor are examined in the context of damage, repair and aging. By outlining the many base excision repair-related mysteries that have yet to be unraveled, hopefully this perspective will stimulate further interest in the field.

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Long-patch BER involves the resynthesis of a longer fragment of DNA, up to 13 nucleotides.
“long-patch BER involves the resynthesis of longer (up to 13 nucleotides) fragment of DNA molecule.”
From Focus on UV-Induced DNA Damage and Repair—Disease Relevance and Protective Strategies (2020) · cites this paper as [113]
In long-patch BER, DNA ligase I ligates the break.
“Finally, DNA ligase I ligates the break in long-patch BER [25,113,114].”
From Focus on UV-Induced DNA Damage and Repair—Disease Relevance and Protective Strategies (2020) · cites this paper as [113]
In short-patch BER, the ligation process is carried out by DNA ligase III working together with its cofactor XRCC1.
“The ligation process is carried by DNA ligase III working together with its cofactor X-ray repair cross-complementing protein 1(XRCC1) [111,112,113].”
From Focus on UV-Induced DNA Damage and Repair—Disease Relevance and Protective Strategies (2020) · cites this paper as [113]

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Saha, T., Rih, J. K., Roy, R., Ballal, R. D., & Rosen, E. M. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.104430 · Cited by 90 · see citing works
The DNA trackwalkers: Principles of lesion search and recognition by DNA glycosylases
Zharkov, D. O., & Grollman, A. P. (2005) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2005.03.011 · Cited by 90 · see citing works
Neil3, the final frontier for the DNA glycosylases that recognize oxidative damage
Liu, M., Doublié, S., & Wallace, S. S. (2012) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2012.12.003 · Cited by 89 · see citing works
Self-citation
Novel Role of Base Excision Repair in Mediating Cisplatin Cytotoxicity
Kothandapani, A., Dangeti, V. S. M. N., Brown, A. R., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.225375 · Cited by 88 · see citing works
Human AP endonuclease (APE1) demonstrates endonucleolytic activity against AP sites in single-stranded DNA
Marenstein, D. R., Wilson, D. M., & Teebor, G. W. (2004) · DNA repair · doi:10.1016/j.dnarep.2004.01.010 · Cited by 85 · see citing works
DNA glycosylase encoded by <i>MUTYH</i> functions as a molecular switch for programmed cell death under oxidative stress to suppress tumorigenesis
Oka, S., & Nakabeppu, Y. (2011) · Cancer Science · doi:10.1111/j.1349-7006.2011.01869.x · Cited by 84 · see citing works
Emerging Roles of the Nucleolus in Regulating the DNA Damage Response: The Noncanonical DNA Repair Enzyme APE1/Ref-1 as a Paradigmatical Example
Antoniali, G., Lirussi, L., Poletto, M., & Tell, G. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5491 · Cited by 84 · see citing works
Evidence for the Involvement of Nucleotide Excision Repair in the Removal of Abasic Sites in Yeast
Torres‐Ramos, C. A., Johnson, R. E., Prakash, L., & Prakash, S. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.10.3522-3528.2000 · Cited by 84 · see citing works
Initiation of Base Excision Repair of Oxidative Lesions in Nucleosomes by the Human, Bifunctional DNA Glycosylase NTH1
Prasad, A., Wallace, S. S., & Pederson, D. S. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00791-07 · Cited by 83 · see citing works
Self-citation
DNA strand break repair and neurodegeneration
Rulten, S. L., & Caldecott, K. W. (2013) · DNA repair · doi:10.1016/j.dnarep.2013.04.008 · Cited by 81 · see citing works
8-Oxoguanine DNA glycosylase-1 links DNA repair to cellular signaling via the activation of the small GTPase Rac1
Hajas, G., Bácsi, A., Aguilera-Aguirre, L., Hegde, M. L., Tapas, K. H., Sur, S. A., Radak, Z. O., Ba, X., & Boldogh, I. R. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.04.011 · Cited by 81 · see citing works
A Germline Polymorphism of DNA Polymerase Beta Induces Genomic Instability and Cellular Transformation
Yamtich, J., Nemec, A. A., Keh, A., & Sweasy, J. B. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1003052 · Cited by 80 · see citing works
Processivity of Escherichia coli and Rat Liver Mitochondrial Uracil-DNA Glycosylase Is Affected by NaCl Concentration
Bennett, S. E., Sanderson, R. J., & Mosbaugh, D. W. (1995) · Biochemistry · doi:10.1021/bi00018a014 · Cited by 79 · see citing works
DNA Demethylation by TDG
Dalton, S. R., & Bellacosa, A. (2012) · Epigenomics · doi:10.2217/epi.12.36 · Cited by 77 · see citing works
Is Base Excision Repair a Tumor Suppressor Mechanism?
Sweasy, J. B., Lang, T., & DiMaio, D. (2006) · Cell Cycle · doi:10.4161/cc.5.3.2414 · Cited by 77 · see citing works
Structure and potential mutagenicity of new hydantoin products from guanosine and 8-oxo-7,8-dihydroguanine oxidation by transition metals.
Burrows, C. J., Muller, J. G., Kornyushyna, O., Luo, W., Duarte, V., Leipold, M. D., & David, S. S. (2002) · Environmental Health Perspectives · doi:10.1289/ehp.02110s5713 · Cited by 75 · see citing works
Variant base excision repair proteins: Contributors to genomic instability
Nemec, A. A., Wallace, S. S., & Sweasy, J. B. (2010) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2010.10.010 · Cited by 74 · see citing works
Self-citation
Hopping Enables a DNA Repair Glycosylase To Search Both Strands and Bypass a Bound Protein
Hedglin, M., & O’Brien, P. (2010) · ACS Chemical Biology · doi:10.1021/cb1000185 · Cited by 72 · see citing works
Base excision repair fidelity in normal and cancer cells
Chan, K. K. L., Zhang, Q.-M., & Dianov, G. L. (2006) · Mutagenesis · doi:10.1093/mutage/gel020 · Cited by 71 · see citing works
DNA polymerase β
Idriss, H. T., Al‐Assar, O., & Wilson, S. H. (2002) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(01)00131-5 · Cited by 69 · see citing works
Activation of cellular signaling by 8-oxoguanine DNA glycosylase-1-initiated DNA base excision repair
Germán, P., Szaniszlo, P., Hajas, G., Radak, Z. O., Bácsi, A., Hazra, T. K., Hegde, M. L., Ba, X., & Boldogh, I. R. (2013) · DNA repair · doi:10.1016/j.dnarep.2013.06.006 · Cited by 68 · see citing works
XRCC1 coordinates disparate responses and multiprotein repair complexes depending on the nature and context of the DNA damage
Hanssen‐Bauer, A., Solvang‐Garten, K., Sundheim, O., Peña-Dı́az, J., Andersen, S. B., Slupphaug, G., Krokan, H. E., Wilson, D. M., Akbari, M., & Otterlei, M. (2011) · Environmental and Molecular Mutagenesis · doi:10.1002/em.20663 · Cited by 68 · see citing works
DNA Repair at Telomeres: Keeping the Ends IntactPreprint
Webb, C. J., Wu, Y., & Zakian, V. A. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a012666 · Cited by 68 · see citing works
Essential role for mammalian apurinic/apyrimidinic (AP) endonuclease Ape1/Ref-1 in telomere maintenance
Madlener, S., Ströbel, T., Vose, S. C., Saydam, O., Price, B. D., Demple, B., & Saydam, N. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1304784110 · Cited by 67 · see citing works
Ubiquitin ligase UBR3 regulates cellular levels of the essential DNA repair protein APE1 and is required for genome stability
Meisenberg, C., Tait, P. S., Dianova, I. I., Wright, K. E., Edelmann, M. J., Ternette, N., Tasaki, T., Kessler, B. M., Parsons, J. L., Kwon, Y. T., et al. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr744 · Cited by 66 · see citing works
DNA Ligase I, the Replicative DNA Ligase
Howes, T. R., & Tomkinson, A. E. (2012) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-94-007-4572-8_17 · Cited by 64 · see citing works
Telomere Repeat Binding Factor 2 Interacts with Base Excision Repair Proteins and Stimulates DNA Synthesis by DNA Polymerase β
Müftüoğlu, M., Wong, H. K., Imam, S. Z., Wilson, D. M., Bohr, V. A., & Opresko, P. L. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-2742 · Cited by 62 · see citing works
Mutation of POLB Causes Lupus in Mice
Senejani, A. G., Liu, Y., Kidane, D., Maher, S. E., Zeiss, C. J., Park, H.-J., Kashgarian, M. J., McNiff, J. M., Zelterman, D. A., Bothwell, A. L. M., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2013.12.017 · Cited by 62 · see citing works
Endonucleolytic incision of x-irradiated deoxyribonucleic acid by extracts of Escherichia coli.
Strniste, G. F., & Wallace, S. S. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.6.1997 · Cited by 60 · see citing works
Self-citation
Defective Repair of Oxidative Base Lesions by the DNA Glycosylase Nth1 Associates with Multiple Telomere Defects
Vallabhaneni, H., O’Callaghan, N. J., Sidorova, J. M., & Liu, Y. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003639 · Cited by 60 · see citing works
A review of recent experiments on step-to-step “hand-off” of the DNA intermediates in mammalian base excision repair pathways
Prasad, R., Beard, W. A., Batra, V. K., Liu, Y., Shock, D. D., & Wilson, S. H. (2011) · Molecular Biology · doi:10.1134/s0026893311040091 · Cited by 60 · see citing works
Different structural states in oligonucleosomes are required for early versus late steps of base excision repair
Nakanishi, S., Prasad, R., Wilson, S. H., & Smerdon, M. J. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm436 · 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
Role of nucleotide excision repair proteins in oxidative DNA damage repair: an updating
Pascucci, B., D’Errico, M., Parlanti, E., Giovannini, S., & Eugenia Dogliotti, Y. (2011) · Biochemistry (Moscow) · doi:10.1134/s0006297911010032 · Cited by 58 · see citing works
Structure and function of the DNA ligases encoded by the mammalian LIG3 gene
Tomkinson, A. E., & Sallmyr, A. (2013) · Gene · doi:10.1016/j.gene.2013.08.061 · Cited by 57 · see citing works
Non-specific DNA binding interferes with the efficient excision of oxidative lesions from chromatin by the human DNA glycosylase, NEIL1
Odell, I. D., Newick, K., Heintz, N. H., Wallace, S. S., & Pederson, D. S. (2009) · DNA repair · doi:10.1016/j.dnarep.2009.11.005 · Cited by 56 · see citing works
Self-citation
The roles of APE1, APE2, DNA polymerase β and mismatch repair in creating S region DNA breaks during antibody class switch
Schrader, C. E., Guikema, J. E. J., Wu, X., & Stavnezer, J. (2008) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2008.0200 · Cited by 56 · see citing works
Oxidants in signal transduction: impact on DNA integrity and gene expression
Ziel, K. A., Grishko, V. I., Campbell, C. C., Breit, J. F., Wilson, G. L., & Gillespie, M. N. (2005) · The FASEB Journal · doi:10.1096/fj.04-2805com · Cited by 55 · see citing works
Structural and biochemical studies of a plant formamidopyrimidine-DNA glycosylase reveal why eukaryotic Fpg glycosylases do not excise 8-oxoguanine
Duclos, S., Aller, P., Jaruga, P., Dizdaroğlu, M., Wallace, S. S., & Doublié, S. (2012) · DNA repair · doi:10.1016/j.dnarep.2012.06.004 · Cited by 54 · see citing works
Self-citation
Germ-line variant of human NTH1 DNA glycosylase induces genomic instability and cellular transformation
Galick, H. A., Kathe, S. D., Liu, M., Robey-Bond, S. M., Kidane, D., Wallace, S. S., & Sweasy, J. B. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1306752110 · Cited by 53 · see citing works
Self-citation
Structural Characterization of Viral Ortholog of Human DNA Glycosylase NEIL1 Bound to Thymine Glycol or 5-Hydroxyuracil-containing DNA
Imamura, K., Averill, A. M., Wallace, S. S., & Doublié, S. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.315309 · Cited by 53 · see citing works
Self-citation
Escherichia coli MutY and Fpg Utilize a Processive Mechanism for Target Location
Francis, A. W., & David, S. S. (2002) · Biochemistry · doi:10.1021/bi026375+ · Cited by 51 · see citing works
Does DNA repair occur during somatic hypermutation?
Saribasak, H., & Gearhart, P. J. (2012) · Seminars in Immunology · doi:10.1016/j.smim.2012.05.002 · Cited by 51 · see citing works
Base Excision Repair Facilitates a Functional Relationship Between Guanine Oxidation and Histone Demethylation
Li, J., Braganza, A., & Sobol, R. W. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.5107 · Cited by 50 · see citing works
Noncoding RNAs in DNA Repair and Genome Integrity
Wan, G., Liu, Y., Han, C., Zhang, X., & Lu, X. (2014) · Antioxidants & Redox Signaling · doi:10.1089/ars.2013.5514 · Cited by 50 · see citing works
Regulation of DNA glycosylases and their role in limiting disease
Sampath, H., McCullough, A. K., & Lloyd, R. S. (2012) · Free Radical Research · doi:10.3109/10715762.2012.655730 · Cited by 49 · see citing works
The Disordered C-Terminal Domain of Human DNA Glycosylase NEIL1 Contributes to Its Stability via Intramolecular Interactions
Hegde, M. L., Tsutakawa, S. E., Hegde, P. M., Holthauzen, L. M. F., Li, J., Oezguen, N., Hilser, V. J., Tainer, J. A., & MITRA, S. P. (2013) · Journal of Molecular Biology · doi:10.1016/j.jmb.2013.03.030 · Cited by 47 · see citing works
Structural Characterization of a Viral NEIL1 Ortholog Unliganded and Bound to Abasic Site-containing DNA
Imamura, K., Wallace, S. S., & Doublié, S. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.021907 · Cited by 45 · see citing works
Self-citation
Genome and cancer single nucleotide polymorphisms of the human NEIL1 DNA glycosylase: Activity, structure, and the effect of editing
Prakash, A., Carroll, B. L., Sweasy, J. B., Wallace, S. S., & Doublié, S. (2014) · DNA repair · doi:10.1016/j.dnarep.2013.12.003 · Cited by 44 · see citing works
Self-citation
Coordination of DNA repair by NEIL1 and PARP-1: a possible link to aging
Noren Hooten, N., Fitzpatrick, M., Kompaniez, K., Jacob, K. D., Moore, B. R., Nagle, J., Barnes, J., Lohani, A., & Evans, M. K. (2012) · Aging · doi:10.18632/aging.100492 · Cited by 44 · see citing works
Binding of the human nucleotide excision repair proteins XPA and XPC/HR23B to the 5 R -thymine glycol lesion and structure of the cis -(5 R ,6 S ) thymine glycol epimer in the 5′-GTgG-3′ sequence: destabilization of two base pairs at the lesion site
Brown, K. L., Roginskaya, M., Zou, Y., Altamirano, A. M., Basu, A. K., & Stone, M. P. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp844 · Cited by 43 · see citing works
Colon Cancer-associated DNA Polymerase β Variant Induces Genomic Instability and Cellular Transformation
Nemec, A. A., Donigan, K. A., Murphy, D. L., Jäger, J., & Sweasy, J. B. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.362111 · Cited by 43 · see citing works
Telomere proteins POT1, TRF1 and TRF2 augment long-patch base excision repair in vitro
Miller, A. S., Balakrishnan, L., Buncher, N. A., Opresko, P. L., & Bambara, R. A. (2012) · Cell Cycle · doi:10.4161/cc.11.5.19483 · Cited by 42 · see citing works
Expression of the Oxidative Base Excision Repair Enzymes is not Induced in TK6 Human Lymphoblastoid Cells after Low Doses of Ionizing Radiation
Inoue, M., Shen, G.-P., Chaudhry, M. A., et al. (2004) · Radiation Research · doi:10.1667/3163 · Cited by 42 · see citing works
Alkyladenine DNA glycosylase (AAG) localizes to mitochondria and interacts with mitochondrial single-stranded binding protein (mtSSB)
van Loon, B., & Samson, L. D. (2013) · DNA repair · doi:10.1016/j.dnarep.2012.11.009 · Cited by 38 · see citing works
DNA Polymerase β Interacts with TRF2 and Induces Telomere Dysfunction in a Murine Mammary Cell Line
Fotiadou, P. P., Henegariu, O., & Sweasy, J. B. (2004) · Cancer Research · doi:10.1158/0008-5472.can-04-0136 · Cited by 37 · see citing works
Contribution of DNA unwrapping from histone octamers to the repair of oxidatively damaged DNA in nucleosomes
Maher, R. L., Prasad, A., Rizvanova, O., Wallace, S. S., & Pederson, D. S. (2013) · DNA repair · doi:10.1016/j.dnarep.2013.08.010 · Cited by 34 · see citing works
Self-citation
Insights into the glycosylase search for damage from single-molecule fluorescence microscopy
Lee, A. J., Warshaw, D. M., & Wallace, S. S. (2014) · DNA repair · doi:10.1016/j.dnarep.2014.01.007 · Cited by 34 · see citing works
Self-citation
DNA-repair in mild cognitive impairment and Alzheimer's disease
Bucholtz, N., & Demuth, I. (2013) · DNA Repair · doi:10.1016/j.dnarep.2013.07.005 · Cited by 34 · see citing works
Telomere protein complexes and interactions with telomerase in telomere maintenance
Pinto, A. R. (2010) · Frontiers in bioscience · doi:10.2741/3683 · Cited by 34 · see citing works
NEIL1 Responds and Binds to Psoralen-induced DNA Interstrand Crosslinks
McNeill, D. R., Paramasivam, M., Baldwin, J., Huang, J., Vyjayanti, V. N., Seidman, M. M., & Wilson, D. M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.456087 · Cited by 29 · see citing works
Correlated Cleavage of Damaged DNA by Bacterial and Human 8-Oxoguanine-DNA Glycosylases
Sidorenko, V. S., & Zharkov, D. O. (2008) · Biochemistry · doi:10.1021/bi800569e · Cited by 28 · see citing works
The Fanconi anemia pathway promotes DNA glycosylase‐dependent excision of interstrand DNA crosslinks
Macé‐Aimé, G., Couvé, S., Khassenov, B., Rosselli, F., & Saparbaev, M. K. (2010) · Environmental and Molecular Mutagenesis · doi:10.1002/em.20548 · Cited by 28 · see citing works
Apurinic/Apyrimidinic Endonuclease 2 Is Necessary for Normal B Cell Development and Recovery of Lymphoid Progenitors after Chemotherapeutic Challenge
Guikema, J. E. J., Gerstein, R. M., Linehan, E. K., Cloherty, E. K., Evan‐Browning, E., Tsuchimoto, D., Nakabeppu, Y., & Schrader, C. E. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1002422 · Cited by 28 · see citing works
Aicardi–Goutières syndrome: clues from the RNase H2 knock-out mouse
Rabe, B. (2013) · Journal of Molecular Medicine · doi:10.1007/s00109-013-1061-x · Cited by 24 · see citing works
The human gastric cancer-associated DNA polymerase β variant D160N is a mutator that induces cellular transformation
Donigan, K. A., Hile, S. E., Eckert, K. A., & Sweasy, J. B. (2012) · DNA repair · doi:10.1016/j.dnarep.2012.01.004 · Cited by 24 · see citing works
A Novel Link to Base Excision Repair
Wilson, D., & Seidman, M. (2010) · TIBS -Trends in Biochemical Sciences. Regular ed · doi:10.1016/j.tibs.2010.01.003 · Cited by 24 · see citing works
AID and Apobec3G haphazard deamination and mutational diversity
Jaszczur, M. M., Bertram, J. G., Pham, P., Scharff, M. D., & Goodman, M. F. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1212-1 · Cited by 24 · see citing works
Consequences and Repair of Oxidative DNA Damage
Duclos, S., Doublié, S., & Wallace, S. S. (2012) · Issues in toxicology · doi:10.1039/9781849732925-00115 · Cited by 22 · see citing works
Self-citation
The E288K Colon Tumor Variant of DNA Polymerase β Is a Sequence Specific Mutator
Murphy, D. L., Donigan, K. A., Jäger, J., & Sweasy, J. B. (2012) · Biochemistry · doi:10.1021/bi3003583 · Cited by 22 · see citing works
The emerging role of Mule and ARF in the regulation of base excision repair
Khoronenkova, S. V., & Dianov, G. L. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.06.015 · Cited by 22 · see citing works
CHIPping Away at Base Excision Repair
Sobol, R. W. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.02.004 · Cited by 21 · see citing works
BRCA1 regulation of base excision repair pathway
Saha, T., Smulson, M. E., & Rosen, E. M. (2010) · Cell Cycle · doi:10.4161/cc.9.13.12084 · Cited by 20 · see citing works
The E295K Cancer Variant of Human Polymerase β Favors the Mismatch Conformational Pathway during Nucleotide Selection
Eckenroth, B. E., Towle-Weicksel, J. B., Sweasy, J. B., & Doublié, S. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.510891 · Cited by 20 · see citing works
mtSSB may sequester UNG1 at mitochondrial ssDNA and delay uracil processing until the dsDNA conformation is restored
Steen, K. W., Doseth, B., Westbye, M. P., Akbari, M., Kang, D., Falkenberg, M., & Slupphaug, G. (2011) · DNA repair · doi:10.1016/j.dnarep.2011.10.026 · Cited by 19 · see citing works
3-Methyladenine DNA glycosylase is important for cellular resistance to psoralen interstrand cross-links
Maor-Shoshani, A., Meira, L. B., Yang, X., & Samson, L. D. (2008) · DNA repair · doi:10.1016/j.dnarep.2008.04.017 · Cited by 15 · see citing works
DNA polymerase β variant Ile260Met generates global gene expression changes related to cellular transformation
Donigan, K. A., Tuck, D. P., Schulz, V., et al. (2012) · Mutagenesis · doi:10.1093/mutage/ges034 · Cited by 5 · see citing works

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5-fluorouracil and other fluoropyrimidines in colorectal cancer: Past, present and future
Vodenkova, S., Buchler, T., Cervena, K., Veskrnova, V., Vodicka, P., & Vymetalkova, V. (2020) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2019.107447 · Cited by 956 · see citing works
Mechanisms and Consequences of Double‐Strand DNA Break Formation in Chromatin
Cannan, W. J., & Pederson, D. S. (2016) · Journal of Cellular Physiology · doi:10.1002/jcp.25048 · Cited by 499 · see citing works
“Most such lesions are subject to base excision repair (BER), which entails production of gapped repair intermediates (for reviews, see David et al., 2007; Hegde et al., 2008; Robertson et al., 2009; Duclos et al., 2012; Krokan and Bjoras, 2013; Wallace, 2014).”
Background
Oxidative DNA damage is epigenetic by regulating gene transcription via base excision repair
Fleming, A. M., Ding, Y., & Burrows, C. J. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1619809114 · Cited by 364 · see citing works
The DNA damage response to transcription stress
Lans, H., Hoeijmakers, J. H. J., Vermeulen, W., & Marteijn, J. A. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0169-4 · Cited by 321 · see citing works
On the wrong DNA track: Molecular mechanisms of repeat-mediated genome instability
Khristich, A. N., & Mirkin, S. M. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.rev119.007678 · Cited by 289 · see citing works
Heat-shock proteins: chaperoning DNA repair
Dubrez, L., Causse, S., Borges Bonan, N., Dumétier, B., & Garrido, C. (2020) · Oncogene · doi:10.1038/s41388-019-1016-y · Cited by 224 · see citing works
Oxidative guanine base damage regulates human telomerase activity
Fouquerel, E., Lormand, J., Bose, A., Lee, H.-T., Kim, G. S., Li, J., Sobol, R. W., Freudenthal, B. D., Myong, S., & Opresko, P. L. (2016) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3319 · Cited by 182 · 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
Somatic and Germline Mutation Periodicity Follow the Orientation of the DNA Minor Groove around Nucleosomes
Pich, O., Muiños, F., Sabarinathan, R., Reyes-Salazar, I., Gonzalez-Perez, A., & Lopez-Bigas, N. (2018) · Cell · doi:10.1016/j.cell.2018.10.004 · Cited by 123 · see citing works
Contributions of DNA Damage to Alzheimer’s Disease
Lin, X., Kapoor, A., Gu, Y., Chow, M. J., Peng, J., Zhao, K., & Tang, D. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21051666 · Cited by 117 · see citing works
Nick-seq for single-nucleotide resolution genomic maps of DNA modifications and damage
Cao, B., Wu, X., Zhou, J., Wu, H., Liu, L., Zhang, Q., DeMott, M. S., Gu, C., Wang, L., You, D., et al. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa473 · Cited by 67 · see citing works
Architects meets Repairers: the interplay between homeobox genes and DNA repair
Feltes, B. C. (2019) · DNA Repair · doi:10.1016/j.dnarep.2018.10.007 · Cited by 15 · see citing works
Base excision repair pathways of bacteria: New promise for an old problem
Kurthkoti, K., Kumar, P., Sang, P. B., & Varshney, U. (2020) · Future Medicinal Chemistry · doi:10.4155/fmc-2019-0267 · Cited by 12 · see citing works

Slow base excision by human alkyladenine DNA glycosylase limits the rate of formation of AP sites and AP endonuclease 1 does not stimulate base excision
Maher, R. L., Vallur, A. C., Feller, J. A., et al. (2006) · DNA repair · doi:10.1016/j.dnarep.2006.09.001 · Cited by 21 · see citing works
AP Endonuclease-Independent DNA Base Excision Repair in Human Cells
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Human AP Endonuclease 1 Stimulates Multiple-Turnover Base Excision by Alkyladenine DNA Glycosylase
Baldwin, M. R., & O’Brien, P. (2009) · Biochemistry · doi:10.1021/bi900517y · Cited by 53 · see citing works
Stimulation of DNA Glycosylase Activity of OGG1 by NEIL1: Functional Collaboration between Two Human DNA Glycosylases
Mokkapati, S. K., Wiederhold, L. R., Hazra, T. K., et al. (2004) · Biochemistry · doi:10.1021/bi049097i · Cited by 77 · see citing works
Base excision repair activities required for yeast to attain a full chronological life span
MacLean, M. J., Aamodt, R. M., Harris, N., Alseth, I., Seeberg, E. C., Bjørås, M., & Piper, P. W. (2003) · Aging Cell · doi:10.1046/j.1474-9728.2003.00041.x · Cited by 43 · see citing works

Authors: Wallace, S. S.
Affiliations: University of Vermont (US)
Corresponding author: Wallace, Susan S.
ORCID: Wallace, Susan S.
Venue: DNA Repair
Publisher: Elsevier BV
Published: 2014-07
Volume: 19
Pages: 14-26
ISSN: 1568-7856 (ISSN-L)
1568-7864
DOI: 10.1016/j.dnarep.2014.03.030
PMC: PMC4100245
OpenAlex: W2016844537
Cited by: 401
References: 165
Citations by year: 2026: 14 · 2025: 26 · 2024: 14 · 2023: 30 · 2022: 39 · 2021: 57 · 2020: 58 · 2019: 44 · 2018: 39 · 2017: 27 · 2016: 24 · 2015: 23 · 2014: 5
FWCI: 10.74
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: DNA repair (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Funders: National Cancer Institute (P01 CA098993)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA and Nucleic Acid Chemistry
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
Keywords: base excision repair, DNA glycosylase, DNA demethylation, transcriptional activation, somatic hypermutation, class switch recombination, retroviral infection, oxidative DNA damage, neurodegenerative diseases, tumor suppression, aging, chromatin, telomeres, post-translational modification, enzyme regulation
MeSH terms: Aging, Chromatin, DNA Damage, DNA Repair, Humans, Methylation, Protein Processing, Post-Translational, Oxidative Stress, DNA Glycosylases

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Base excision repair: A critical player in many games

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