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Journal articles on the topic 'Base excision'

Author: Grafiati

Published: 7 June 2025

Last updated: 16 July 2025

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1

Krokan, H. E., and M. Bjoras. "Base Excision Repair." Cold Spring Harbor Perspectives in Biology 5, no. 4 (2013): a012583. http://dx.doi.org/10.1101/cshperspect.a012583.

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2

Intano, Gabriel W., C. Alex McMahan, John R. McCarrey, et al. "Base Excision Repair Is Limited by Different Proteins in Male Germ Cell Nuclear Extracts Prepared from Young and Old Mice." Molecular and Cellular Biology 22, no. 7 (2002): 2410–18. http://dx.doi.org/10.1128/mcb.22.7.2410-2418.2002.

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ABSTRACT The combined observations of elevated DNA repair gene expression, high uracil-DNA glycosylase-initiated base excision repair, and a low spontaneous mutant frequency for a lacI transgene in spermatogenic cells from young mice suggest that base excision repair activity is high in spermatogenic cell types. Notably, the spontaneous mutant frequency of the lacI transgene is greater in spermatogenic cells obtained from old mice, suggesting that germ line DNA repair activity may decline with age. A paternal age effect in spermatogenic cells is recognized for the human population as well. To determine if male germ cell base excision repair activity changes with age, uracil-DNA glycosylase-initiated base excision repair activity was measured in mixed germ cell (i.e., all spermatogenic cell types in adult testis) nuclear extracts prepared from young, middle-aged, and old mice. Base excision repair activity was also assessed in nuclear extracts from premeiotic, meiotic, and postmeiotic spermatogenic cell types obtained from young mice. Mixed germ cell nuclear extracts exhibited an age-related decrease in base excision repair activity that was restored by addition of apurinic/apyrimidinic (AP) endonuclease. Uracil-DNA glycosylase and DNA ligase were determined to be limiting in mixed germ cell nuclear extracts prepared from young animals. Base excision repair activity was only modestly elevated in pachytene spermatocytes and round spermatids relative to other spermatogenic cells. Thus, germ line short-patch base excision repair activity appears to be relatively constant throughout spermatogenesis in young animals, limited by uracil-DNA glycosylase and DNA ligase in young animals, and limited by AP endonuclease in old animals.

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3

Hawkins, Gregory A., and Les M. Hoffman. "Base excision sequence scanning." Nature Biotechnology 15, no. 8 (1997): 803–4. http://dx.doi.org/10.1038/nbt0897-803.

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4

Zharkov, D. O. "Base excision DNA repair." Cellular and Molecular Life Sciences 65, no. 10 (2008): 1544–65. http://dx.doi.org/10.1007/s00018-008-7543-2.

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5

Dianov, Grigory. "Base excision DNA repair." European Journal of Cancer 29 (January 1993): S32. http://dx.doi.org/10.1016/0959-8049(93)90770-g.

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6

Sidhu, Ashwin. "Base Excision Repair: A Review." Journal of BioMed Research and Reports 2, no. 4 (2023): 1–3. http://dx.doi.org/10.59657/2837-4681.brs.23.032.

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Base excision repair (BER) is a fundamental DNA repair pathway essential for maintaining the genomic integrity of all living organisms. This paper provides an overview of the mechanisms, key players, and regulatory aspects of the base excision repair pathway. BER serves as the primary defense against spontaneous DNA damage arising from endogenous and exogenous sources, including oxidative stress, deamination, and alkylation. This repair process involves a sequential series of enzymatic reactions orchestrated by various proteins, including DNA glycosylases, AP endonucleases, DNA polymerases, and DNA ligases.

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7

Kurthkoti, Krishna, and Umesh Varshney. "Base excision and nucleotide excision repair pathways in mycobacteria." Tuberculosis 91, no. 6 (2011): 533–43. http://dx.doi.org/10.1016/j.tube.2011.06.005.

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8

Agnez-Lima, Lucymara F., Sílvia R. Batistuzzo de Medeiros, Bruno S. Maggi, and Giovanna A. S. Quaresma. "Base excision repair in sugarcane." Genetics and Molecular Biology 24, no. 1-4 (2001): 123–29. http://dx.doi.org/10.1590/s1415-47572001000100017.

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DNA damage can be induced by a large number of physical and chemical agents from the environment as well as compounds produced by cellular metabolism. This type of damage can interfere with cellular processes such as replication and transcription, resulting in cell death and/or mutations. The low frequency of mutagenesis in cells is due to the presence of enzymatic pathways which repair damaged DNA. Several DNA repair genes (mainly from bacteria, yeasts and mammals) have been cloned and their products characterized. The high conservation, especially in eukaryotes, of the majority of genes related to DNA repair argues for their importance in the maintenance of life on earth. In plants, our understanding of DNA repair pathways is still very poor, the first plant repair genes having only been cloned in 1997 and the mechanisms of their products have not yet been characterized. The objective of our data mining work was to identify genes related to the base excision repair (BER) pathway, which are present in the database of the Sugarcane Expressed Sequence Tag (SUCEST) Project. This search was performed by tblastn program. We identified sugarcane clusters homologous to the majority of BER proteins used in the analysis and a high degree of conservation was observed. The best results were obtained with BER proteins from Arabidopsis thaliana. For some sugarcane BER genes, the presence of more than one form of mRNA is possible, as shown by the occurrence of more than one homologous EST cluster.

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9

Maynard, Scott, Nadja C. de Souza-Pinto, Morten Scheibye-Knudsen, and Vilhelm A. Bohr. "Mitochondrial base excision repair assays." Methods 51, no. 4 (2010): 416–25. http://dx.doi.org/10.1016/j.ymeth.2010.02.020.

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10

Seeberg, Erling, Lars Eide, and Magnar Bjørås. "The base excision repair pathway." Trends in Biochemical Sciences 20, no. 10 (1995): 391–97. http://dx.doi.org/10.1016/s0968-0004(00)89086-6.

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11

Wallace, Susan S., Drew L. Murphy, and Joann B. Sweasy. "Base excision repair and cancer." Cancer Letters 327, no. 1-2 (2012): 73–89. http://dx.doi.org/10.1016/j.canlet.2011.12.038.

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12

Mullins, Elwood A., Garrett M. Warren, Noah P. Bradley, and Brandt F. Eichman. "Structure of a DNA glycosylase that unhooks interstrand cross-links." Proceedings of the National Academy of Sciences 114, no. 17 (2017): 4400–4405. http://dx.doi.org/10.1073/pnas.1703066114.

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DNA glycosylases are important editing enzymes that protect genomic stability by excising chemically modified nucleobases that alter normal DNA metabolism. These enzymes have been known only to initiate base excision repair of small adducts by extrusion from the DNA helix. However, recent reports have described both vertebrate and microbial DNA glycosylases capable of unhooking highly toxic interstrand cross-links (ICLs) and bulky minor groove adducts normally recognized by Fanconi anemia and nucleotide excision repair machinery, although the mechanisms of these activities are unknown. Here we report the crystal structure of Streptomyces sahachiroi AlkZ (previously Orf1), a bacterial DNA glycosylase that protects its host by excising ICLs derived from azinomycin B (AZB), a potent antimicrobial and antitumor genotoxin. AlkZ adopts a unique fold in which three tandem winged helix-turn-helix motifs scaffold a positively charged concave surface perfectly shaped for duplex DNA. Through mutational analysis, we identified two glutamine residues and a β-hairpin within this putative DNA-binding cleft that are essential for catalytic activity. Additionally, we present a molecular docking model for how this active site can unhook either or both sides of an AZB ICL, providing a basis for understanding the mechanisms of base excision repair of ICLs. Given the prevalence of this protein fold in pathogenic bacteria, this work also lays the foundation for an emerging role of DNA repair in bacteria-host pathogenesis.

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13

Hurst, Verena, Kiran Challa, Kenji Shimada, and Susan M. Gasser. "Cytoskeleton integrity influences XRCC1 and PCNA dynamics at DNA damage." Molecular Biology of the Cell 32, no. 20 (2021): br6. http://dx.doi.org/10.1091/mbc.e20-10-0680.

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Actin perturbation by latrunculins (Lat) reduces recruitment of base excision repair factors to laser-induced damage, while nocodazole treatment increases it. Surprisingly, LatA leads to the nuclear accumulation of both actin and tubulin. Since actin perturbation aggravates Zeocin-induced cell death, this links cytoskeletal integrity to base excision repair.

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14

Legrand, Melanie, Christine L. Chan, Peter A. Jauert, and David T. Kirkpatrick. "Analysis of base excision and nucleotide excision repair in Candida albicans." Microbiology 154, no. 8 (2008): 2446–56. http://dx.doi.org/10.1099/mic.0.2008/017616-0.

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15

Goutos, Ioannis. "Intralesional excision as a surgical strategy to manage keloid scars: what’s the evidence?" Scars, Burns & Healing 5 (January 2019): 205951311986729. http://dx.doi.org/10.1177/2059513119867297.

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Introduction: Keloid scars are a particularly challenging clinical entity and a variety of management approaches have been described in the literature including intralesional surgery. The current literature lacks a summative review to ascertain the evidence base behind this surgical approach. Methods: A comprehensive English literature database search was performed using PubMed Medline, EMBASE and Web of Science from their individual dates of inception to March 2018. We present the different rationales proposed for the use of this technique, the clinical outcomes reported in the literature as well as the scientific basis for intralesional excision of keloid scars. Discussion: A number of arguments have been proposed to support intralesional excision including avoiding injury to neighbouring non-keloidal skin and the deep layer of the dermis, removal of the most proliferative fibroblastic group as well as debulking to facilitate the administration of injectable steroid. The most current literature does not provide sufficient support for the adoption of intralesional excisions based on data emerging from basic science as well as clinical outcome studies. Conclusion: Emerging evidence supports the extralesional excision of keloid scars based on current mechanobiological, histological as well as clinical outcome data. Further trials comparing extralesional and intralesional surgical practices are eagerly awaited to ascertain the role of intralesional excisions in the keloid management arena.

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16

Faheem, Mohd, Raj Kumar, and Hanuman Prasad Prajapati. "Extended Frontobasal Approach for Skull Base Lesions." Indian Journal of Neurosurgery 10, no. 01 (2021): 049–53. http://dx.doi.org/10.1055/s-0040-1716931.

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Abstract Background Lesions involving the skull base can be approached by a variety of surgical corridors and extended frontobasal approach is one of them. It provides quite a wide exposure to lesions in the midline of anterior skull base, paranasal sinuses, and sphenoclival region. Objective To share our experience, and list the merits and demerits, of this approach for anterior skull base lesions. Methods A total of six cases were operated using extended frontobasal approach. Four of them were skull base tumors with extensive involvement of paranansal sinuses and extension into sellar, parasellar, and clival region. Fronto-orbital and sphenoethmoidal osteotomy provided adequate surgical access, thereby facilitating their excision. Two cases of frontonaso-orbital encephalocele with large bone defect at anterior skull base were also operated upon. Skull base repair was performed using autologous bone graft, pericranium, and fibrin glue. Results Gross total excision was achieved in four cases of skull base tumors with good cosmesis as transfacial access was obviated. Excision, repair, and reconstruction of two patients with frontonaso-orbital encephalocele were also done with acceptable cosmesis. Conclusion The extended frontobasal approach is an excellent alternative for extensive anterior skull base tumors (up to posterior skull base), and also for the repair of large malformative lesions of the anterior skull base.

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17

Kwiatkowski, Dominik, and Tomasz Śliwiński. "Base excision repair in Alzheimer’s disease." Postępy Higieny i Medycyny Doświadczalnej 68 (July 22, 2014): 976–86. http://dx.doi.org/10.5604/17322693.1114036.

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18

Adhikari, Sanjay, Sujata Choudhury, Partha Mitra, Jerita Dubash, Shyama Sajankila, and Rabindra Roy. "Targeting Base Excision Repair for Chemosensitization." Anti-Cancer Agents in Medicinal Chemistry 8, no. 4 (2008): 351–57. http://dx.doi.org/10.2174/187152008784220366.

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19

Kim, Yun-Jeong, and David M. Wilson III. "Overview of Base Excision Repair Biochemistry." Current Molecular Pharmacology 5, no. 1 (2012): 3–13. http://dx.doi.org/10.2174/1874467211205010003.

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20

Tell, Gianluca, and Bruce Demple. "Base excision DNA repair and cancer." Oncotarget 6, no. 2 (2014): 584–85. http://dx.doi.org/10.18632/oncotarget.2705.

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21

Malta, Erik, Geri F. Moolenaar, and Nora Goosen. "Base Flipping in Nucleotide Excision Repair." Journal of Biological Chemistry 281, no. 4 (2005): 2184–94. http://dx.doi.org/10.1074/jbc.m508901200.

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22

Srivastava, Deepak K., Brian J. Vande Berg, Rajendra Prasad, et al. "Mammalian Abasic Site Base Excision Repair." Journal of Biological Chemistry 273, no. 33 (1998): 21203–9. http://dx.doi.org/10.1074/jbc.273.33.21203.

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23

Noble, Christian. "Base excision repair gets a refit." Trends in Biochemical Sciences 27, no. 5 (2002): 228. http://dx.doi.org/10.1016/s0968-0004(02)02120-5.

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24

Sobol, Robert W. "CHIPping Away at Base Excision Repair." Molecular Cell 29, no. 4 (2008): 413–15. http://dx.doi.org/10.1016/j.molcel.2008.02.004.

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25

Wilson, David M., Daemyung Kim, Brian R. Berquist, and Alice J. Sigurdson. "Variation in base excision repair capacity." Mutation Research/Fundamental and Molecular Mechanisms of Mutagenesis 711, no. 1-2 (2011): 100–112. http://dx.doi.org/10.1016/j.mrfmmm.2010.12.004.

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26

Lindahl, Tomas. "Inroads into base excision repair I." DNA Repair 3, no. 11 (2004): 1521–30. http://dx.doi.org/10.1016/j.dnarep.2004.05.013.

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27

Friedberg, Errol C. "Inroads into base excision repair II." DNA Repair 3, no. 11 (2004): 1531–36. http://dx.doi.org/10.1016/j.dnarep.2004.05.014.

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28

Jagannathan, Indu, Hope A. Cole, and Jeffrey J. Hayes. "Base excision repair in nucleosome substrates." Chromosome Research 14, no. 1 (2006): 27–37. http://dx.doi.org/10.1007/s10577-005-1020-7.

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29

Korolev, V. G. "Base Excision Repair of DNA: Glycosylases." Russian Journal of Genetics 41, no. 6 (2005): 583–92. http://dx.doi.org/10.1007/s11177-005-0131-8.

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30

Kennedy, Erin E., Paul J. Caffrey, and Sarah Delaney. "Initiating base excision repair in chromatin." DNA Repair 71 (November 2018): 87–92. http://dx.doi.org/10.1016/j.dnarep.2018.08.011.

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31

TALPAERT-BORLÉ, Myriam, and Michel LIUZZI. "Base-Excision Repair in Carrot Cells." European Journal of Biochemistry 124, no. 3 (2005): 435–40. http://dx.doi.org/10.1111/j.1432-1033.1982.tb06611.x.

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32

Prakash, Aishwarya, and Sylvie Doublié. "Base Excision Repair in the Mitochondria." Journal of Cellular Biochemistry 116, no. 8 (2015): 1490–99. http://dx.doi.org/10.1002/jcb.25103.

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33

Ripon, Khalipha Abul Bashar. "Natural compounds in prostate cancer therapy: In silico study." Natural compounds in prostate cancer therapy: In silico study 2, no. 1 (2025): 1–17. https://doi.org/10.5281/zenodo.15052940.

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<strong>Abstract</strong>Among males all over the world, the most common non-cutanous cancer in man is prostate cancer. Although localized prostate cancer has a greater long-term survival probability, metastatic prostate cancer is almost always incurable, even after receiving intensive combination therapy. It has been demonstrated that prostate cells express the genes 1CDZ, 1XNA, and 1XNT, and that the proteins that are produced by these genes are responsible for base excision repair. In a similar manner, the 2D8M and 2W3O genes codify for the protein that is accountable for the repair of nucleotide excision. Furthermore, the 3K75 enzyme, which is encoded by the 3K75 gene, sustains the integrity of the genome. To identifying potentially effective inhibitors against prostate cancer, we have conducted an analysis of several natural substances that show promise. Techniques: Molecular docking techniques were utilized to test various compounds against proteins that were encoded by the 1CDZ, 2D8M, 2W3O, 1XNT, and 3K75 genes utilizing various chemicals. According to the findings, out of all the compounds that were utilized, five of them (Oleanolic Acid, Brusatol, Agroclavine, Genistein, and Asiaticoside) have demonstrated the highest binding affinity energy against the protein targets 1CDZ, 1XNA, 2D8M, 2W3O, and 3K75. Conclusion: Based on the findings of our in-silico research, we are able to confidently draw the conclusion that the chemicals described above exhibit superior anti-cancer efficacy against prostate cancer. <strong>Keywords:</strong> Natural compounds; Prostate cancer; DNA damage; Base excision; Mutation; 1CDZ; 1XNA; 2D8M; 2W3O; 3K75. <strong>List of abbreviation:</strong>1CDZ: X-ray repair cross-complementing group1, 1XNA: X-ray repair cross-complementing group 3, 2D8M: Excision Repair Cross-Complementation Group 1, 2W3O: Excision Repair Cross Complementation Group 2, 1XNT: human oxoguanine glycosylase 1, BER: base excision repair, NER: nucleotide excision repair.

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34

Zhu, Chenxu, Lining Lu, Jun Zhang, et al. "Tautomerization-dependent recognition and excision of oxidation damage in base-excision DNA repair." Proceedings of the National Academy of Sciences 113, no. 28 (2016): 7792–97. http://dx.doi.org/10.1073/pnas.1604591113.

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NEIL1 (Nei-like 1) is a DNA repair glycosylase guarding the mammalian genome against oxidized DNA bases. As the first enzymes in the base-excision repair pathway, glycosylases must recognize the cognate substrates and catalyze their excision. Here we present crystal structures of human NEIL1 bound to a range of duplex DNA. Together with computational and biochemical analyses, our results suggest that NEIL1 promotes tautomerization of thymine glycol (Tg)—a preferred substrate—for optimal binding in its active site. Moreover, this tautomerization event also facilitates NEIL1-catalyzed Tg excision. To our knowledge, the present example represents the first documented case of enzyme-promoted tautomerization for efficient substrate recognition and catalysis in an enzyme-catalyzed reaction.

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35

Kreppel, Andrea, Iris D. Blank, and Christian Ochsenfeld. "Base-Independent DNA Base-Excision Repair of 8-Oxoguanine." Journal of the American Chemical Society 140, no. 13 (2018): 4522–26. http://dx.doi.org/10.1021/jacs.7b11254.

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36

McKinney, P. "Nasal Base Narrowing: The Combined Alar Base Excision Technique." Yearbook of Plastic and Aesthetic Surgery 2008 (January 2008): 130–31. http://dx.doi.org/10.1016/s1535-1513(08)70599-x.

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37

Gary, Ronald, Kyung Kim, Helen L. Cornelius, Min S. Park, and Yoshihiro Matsumoto. "Proliferating Cell Nuclear Antigen Facilitates Excision in Long-patch Base Excision Repair." Journal of Biological Chemistry 274, no. 7 (1999): 4354–63. http://dx.doi.org/10.1074/jbc.274.7.4354.

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38

Ma, Xiaodi, Hewei Ming, Lexin Liu, et al. "OGG1 in Lung—More than Base Excision Repair." Antioxidants 11, no. 5 (2022): 933. http://dx.doi.org/10.3390/antiox11050933.

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As the organ executing gas exchange and directly facing the external environment, the lungs are challenged continuously by various stimuli, causing the disequilibration of redox homeostasis and leading to pulmonary diseases. The breakdown of oxidants/antioxidants system happens when the overproduction of free radicals results in an excess over the limitation of cleaning capability, which could lead to the oxidative modification of macromolecules including nucleic acids. The most common type of oxidative base, 8-oxoG, is considered the marker of DNA oxidative damage. The appearance of 8-oxoG could lead to base mismatch and its accumulation might end up as tumorigenesis. The base 8-oxoG was corrected by base excision repair initiated by 8-oxoguanine DNA glycosylase-1 (OGG1), which recognizes 8-oxoG from the genome and excises it from the DNA double strand, generating an AP site for further processing. Aside from its function in DNA damage repairment, it has been reported that OGG1 takes part in the regulation of gene expression, derived from its DNA binding characteristic, and showed impacts on inflammation. Researchers believe that OGG1 could be the potential therapy target for relative disease. This review intends to make an overall summary of the mechanism through which OGG1 regulates gene expression and the role of OGG1 in pulmonary diseases.

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39

Sen, Chandranath, and Aymara Triana. "Cranial chordomas: results of radical excision." Neurosurgical Focus 10, no. 3 (2001): 1–7. http://dx.doi.org/10.3171/foc.2001.10.3.4.

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Object The authors analyze their experience with the treatment of 29 patients who underwent radical excision of skull base chordomas. Methods Modern skull base surgical techniques were used in all patients who were treated between August 1991 and July 2000. The degree of tumor resection was gauged according to intraoperative inspection and postoperative high-resolution imaging findings. There were 21 patients with primary disease and eight with recurrent disease. Total resection was accomplished in 18 patients. Five patients had undergone radiotherapy prior to the present surgery, and an additional eight patients underwent postoperative radiotherapy. There were no surgery-related deaths. In five patients who died of the disease, surgery and radiotherapy had failed to effect a cure. Two of the remaining patients are alive with recurrent disease, and there is questionable evidence of recurrence in another patient. All 24 patients are functioning independently. Cranial nerve impairment was the most common postoperative deficit, followed by cerebrospinal fluid (CSF) leakage and infection. Conclusions The use of skull base techiniques in radical surgery provides an opportunity to excise the tumor and the involved bone. In most cases the procedure-related cranial nerve deficits improve over time. The complications of CSF leakage and infection can be minimized and are preventable. Proton beam irradiation is an excellent adjuvant treatment but is reserved for patients with definite tumor recurrence or residual tumor that can be identified on the imaging studies.

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40

Sharma, Priti, Swosti S. Das, Maneesh Mishra, and Mala Trivedi. "A novel in vitro shoot excision technique for enhancing proliferation in banana cv. Chini Champa." Journal of Applied Horticulture 26, no. 02 (2024): 258–61. http://dx.doi.org/10.37855/jah.2024.v26i02.49.

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Micropropagation technology has been commercially exploited for mass multiplication of banana. Several parameters such as nutrient media, explants, culture conditions etc have been standardized. However, a novel in vitro shoot excision technique designed to enhance the proliferation rate of banana cv. Chini Champa has been examined for the first time. We meticulously examined the impact of excision angles (45º and 90º) and excision site (Tip, middle and base) during shoot proliferation stage. Our findings unequivocally demonstrate that employing a 45º angle excision and tip excision yield the highest multiplication rates and biomass accumulation, surpassing other excision angles and methods. The substantial enhancement in shoot numbers, growth and biomass underscores the potential of this technique for improving banana propagation protocols, offering a valuable tool for sustainable banana production.

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41

KROKAN, Hans E., Rune STANDAL, and Geir SLUPPHAUG. "DNA glycosylases in the base excision repair of DNA." Biochemical Journal 325, no. 1 (1997): 1–16. http://dx.doi.org/10.1042/bj3250001.

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A wide range of cytotoxic and mutagenic DNA bases are removed by different DNA glycosylases, which initiate the base excision repair pathway. DNA glycosylases cleave the N-glycosylic bond between the target base and deoxyribose, thus releasing a free base and leaving an apurinic/apyrimidinic (AP) site. In addition, several DNA glycosylases are bifunctional, since they also display a lyase activity that cleaves the phosphodiester backbone 3′ to the AP site generated by the glycosylase activity. Structural data and sequence comparisons have identified common features among many of the DNA glycosylases. Their active sites have a structure that can only bind extrahelical target bases, as observed in the crystal structure of human uracil-DNA glycosylase in a complex with double-stranded DNA. Nucleotide flipping is apparently actively facilitated by the enzyme. With bacteriophage T4 endonuclease V, a pyrimidine-dimer glycosylase, the enzyme gains access to the target base by flipping out an adenine opposite to the dimer. A conserved helix–hairpin–helix motif and an invariant Asp residue are found in the active sites of more than 20 monofunctional and bifunctional DNA glycosylases. In bifunctional DNA glycosylases, the conserved Asp is thought to deprotonate a conserved Lys, forming an amine nucleophile. The nucleophile forms a covalent intermediate (Schiff base) with the deoxyribose anomeric carbon and expels the base. Deoxyribose subsequently undergoes several transformations, resulting in strand cleavage and regeneration of the free enzyme. The catalytic mechanism of monofunctional glycosylases does not involve covalent intermediates. Instead the conserved Asp residue may activate a water molecule which acts as the attacking nucleophile.

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42

Saha, Tapas, Mark Smulson, and Eliot M. Rosen. "BRCA1 regulation of base excision repair pathway." Cell Cycle 9, no. 13 (2010): 2471–72. http://dx.doi.org/10.4161/cc.9.13.12084.

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43

G. Frosina and G. Frosina. "Tumor Suppression by DNA Base Excision Repair." Mini-Reviews in Medicinal Chemistry 7, no. 7 (2007): 727–43. http://dx.doi.org/10.2174/138955707781024544.

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44

Dianov, Grigory L., and Ulrich Hübscher. "Mammalian Base Excision Repair: the Forgotten Archangel." Nucleic Acids Research 41, no. 6 (2013): 3483–90. http://dx.doi.org/10.1093/nar/gkt076.

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45

WILSON, S. H., R. W. SOBOL, W. A. BEARD, J. K. HORTON, R. PRASAD, and B. J. VANDE BERG. "DNA Polymerase and Mammalian Base Excision Repair." Cold Spring Harbor Symposia on Quantitative Biology 65 (January 1, 2000): 143–56. http://dx.doi.org/10.1101/sqb.2000.65.143.

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46

David, Sheila S., Valerie L. O'Shea, and Sucharita Kundu. "Base-excision repair of oxidative DNA damage." Nature 447, no. 7147 (2007): 941–50. http://dx.doi.org/10.1038/nature05978.

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47

Foda, Hossam. "Alar Base Reduction: The Boomerang-Shaped Excision." Facial Plastic Surgery 27, no. 02 (2011): 225–34. http://dx.doi.org/10.1055/s-0030-1271302.

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Xu, Guogang, Maryanne Herzig, Vladimir Rotrekl, and Christi A. Walter. "Base excision repair, aging and health span." Mechanisms of Ageing and Development 129, no. 7-8 (2008): 366–82. http://dx.doi.org/10.1016/j.mad.2008.03.001.

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Wilson, David M., and Michael M. Seidman. "A novel link to base excision repair?" Trends in Biochemical Sciences 35, no. 5 (2010): 247–52. http://dx.doi.org/10.1016/j.tibs.2010.01.003.

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Lloyd, R. Stephen. "Base excision repair of cyclobutane pyrimidine dimers." Mutation Research/DNA Repair 408, no. 3 (1998): 159–70. http://dx.doi.org/10.1016/s0921-8777(98)00032-9.

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