Cited by 329DNA Repair MechanismsGenetic factors in colorectal cancerCarcinogens and Genotoxicity Assessment

The DOI matches its Crossref record; 351 of the 357 references it cites were found in a registry or an index.

Base excision repair and cancer

Open access

Wallace, Susan S., Murphy, Drew L., Sweasy, Joann B.·2012·Cancer Letters

DOI 10.1016/j.canlet.2011.12.038PMC PMC3361536

Open this paper in CoChat — free account

Abstract

Base excision repair is the system used from bacteria to man to remove the tens of thousands of endogenous DNA damages produced daily in each human cell. Base excision repair is required for normal mammalian development and defects have been associated with neurological disorders and cancer. In this paper we provide an overview of short patch base excision repair in humans and summarize current knowledge of defects in base excision repair in mouse models and functional studies on short patch base excision repair germ line polymorphisms and their relationship to cancer. The biallelic germ line mutations that result in MUTYH-associated colon cancer are also discussed.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1016/j.canlet.2011.12.038

Cites

351 of 351 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

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
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
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
Genome-wide association study identifies novel breast cancer susceptibility loci
Easton, D. F., Pooley, K. A., Dunning, A. M., Pharoah, P. D. P., Thompson, D., Ballinger, D. G., Struewing, J. P., Morrison, J., Field, H., Luben, R., et al. (2007) · Nature · doi:10.1038/nature05887 · Cited by 2,319
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 1,412
Deletion of a DNA Polymerase β Gene Segment in T Cells Using Cell Type-Specific Gene Targeting
Gu, H., Marth, J. D., Orban, P. C., Mossmann, H., & Rajewsky, K. (1994) · Science · doi:10.1126/science.8016642 · Cited by 1,397
Hereditary and Familial Colon Cancer
Jasperson, K. W., Tuohy, T. M. F., Neklason, D. W., & Burt, R. W. (2010) · Gastroenterology · doi:10.1053/j.gastro.2010.01.054 · Cited by 1,370
Base-excision repair of oxidative DNA damage
David, S. S., O'Shea, V. L., & Kundu, S. (2007) · Nature · doi:10.1038/nature05978 · Cited by 1,238
Single-strand break repair and genetic disease
Caldecott, K. W. (2008) · Nature Reviews Genetics · doi:10.1038/nrg2380 · Cited by 1,097
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

Flagged first, then by citations

Show all 357 references

6 of the 357 references couldn’t be matched to a known paper.

Sorted by citations

Items 201–300 of 327

Density functional theory investigations on the interaction of uracil with borospherene
Kaur, J., Kumar, R., Vohra, R., & Sawhney, R. S. (2022) · Bulletin of Materials Science · doi:10.1007/s12034-021-02595-z · Cited by 8
SUMOylation effects on neural stem cells self-renewal, differentiation, and survival.
Queiroz, L. Y., Kageyama, R., & Cimarosti, H. (2023) · Neurosciences research · doi:10.1016/j.neures.2023.09.006 · Cited by 7
Artemis is required to improve the accuracy of repair of double-strand breaks with 5′-blocked termini generated from non-DSB-clustered lesions
Malyarchuk, S., Castore, R., Shi, R., & Harrison, L. (2013) · Mutagenesis · doi:10.1093/mutage/get009 · Cited by 8
Cell Senescence and the DNA Single-Strand Break Damage Repair Pathway
Sarma, P. A. P., Abbadie, C., de Launoit, Y., & Cleri, F. (2024) · DNA · doi:10.3390/dna4040036 · Cited by 8
The chromatin regulator HELLS mediates SSB repair and responses to DNA alkylation damage
Joseph, J. T., Wright, C. M., Peixoto, E., Shibata, E., Khan, A. U., Li, Y., Neidigk, J. R., Chen, B.-R., Tufail, S., Mujawar, A., et al. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf1201 · Cited by 7
Versatile cell-based assay for measuring DNA alkylation damage and its repair
Li, Y., Mao, P., Basenko, E. Y., Lewis, Z., Smerdon, M. J., & Czaja, W. (2021) · Scientific Reports · doi:10.1038/s41598-021-97523-w · Cited by 7
Production, Purification, and Characterization of 15N-Labeled DNA Repair Proteins as Internal Standards for Mass Spectrometric Measurements
Reddy, P. T., Jaruga, P., Nelson, B. C., Lowenthal, M. S., Jemth, A., Loseva, O., Coşkun, E., Helleday, T., & Dizdaroğlu, M. (2015) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2015.06.044 · Cited by 7
Base and Nucleotide Excision Repair Pathways in DNA Plasmids Harboring Oxidatively Generated Guanine Lesions
Kolbanovskiy, M., Aharonoff, A., Sales, A. H., Geacintov, N. E., & Shafirovich, V. (2021) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.0c00463 · Cited by 7
The R280H X-ray cross-complementing 1 germline variant induces genomic instability and cellular transformation
Sizova, D. V., Keh, A., Taylor, B. F., & Sweasy, J. B. (2015) · DNA repair · doi:10.1016/j.dnarep.2015.05.005 · Cited by 8
Self-citation
Carrier Frequency and Incidence of MUTYH -Associated Polyposis Based on Database Analysis in East Asians and Koreans
Park, J. E., Lee, T., Cho, E. H., Jang, M., Won, D., Park, B., Ki, C., & Kong, S. (2024) · Annals of Laboratory Medicine · doi:10.3343/alm.2024.0242 · Cited by 6
Biological Models of Oxidative Purine DNA Damage in Neurodegenerative Disorders
Chatgilialoglu, C. (2025) · Antioxidants · doi:10.3390/antiox14050578 · Cited by 7
Epigenetic Drivers of Chemoresistance in Nucleobase and Nucleoside Analog Therapies
Kaszycki, J., & Kim, M. (2025) · Biology · doi:10.3390/biology14070838 · Cited by 6
Increased KRAS G12C Prevalence, High Tumor Mutational Burden, and Specific Mutational Signatures Are Associated With MUTYH Mutations: A Pan-Cancer Analysis
Dişel, U., Sivakumar, S., Pham, T. V., Fleischmann, Z., I, A. R., Sokol, E. S., & Kurzrock, R. (2023) · The Oncologist · doi:10.1093/oncolo/oyad230 · Cited by 6
Genetic Polymorphisms in DNA Repair Gene APE1/Ref-1 and the Risk of Neural Tube Defects in a High-Risk Area of China
Wang, X., Yue, H., Shen, L., Guo, J., Guan, Z., Zhu, Z., Niu, B., Zhang, T., & Wang, J. (2021) · Reproductive Sciences · doi:10.1007/s43032-021-00537-y · Cited by 6
Alternative splicing patterns reveal prognostic indicator in muscle-invasive bladder cancer
Azhati, B., Wu, G., Zhan, H., Liang, W. P., Song, Z., Lu, L., & Xie, Q. (2022) · World Journal of Surgical Oncology · doi:10.1186/s12957-022-02685-0 · Cited by 6
Identification of a novel cellular senescence-related signature for the prediction of prognosis and immunotherapy response in colon cancer
Dai, L., Wang, X., Bai, T., Liu, J., Chen, B., Li, T., & Yang, W. (2022) · Frontiers in Genetics · doi:10.3389/fgene.2022.961554 · Cited by 6
DNA glycosylase deficiency leads to decreased severity of lupus in the Polb-Y265C mouse model
Paluri, S. L. A., Burak, M. J., Senejani, A. G., Levinson, M., Rahim, T., Clairmont, K., Kashgarian, M. J., Alvarado-Cruz, I., Meas, R., Cardó‐Vila, M., et al. (2021) · DNA repair · doi:10.1016/j.dnarep.2021.103152 · Cited by 6
Self-citation
Identification of molecular subtypes and prognostic signature for hepatocellular carcinoma based on genes associated with homologous recombination deficiency
Lin, H., Xie, Y., Kong, Y., Yang, L., & Li, M. (2021) · Scientific Reports · doi:10.1038/s41598-021-03432-3 · Cited by 6
Interaction of Arg194Trp and Arg399Gln genotypes with the risk of radiation on cancer patients
Surniyantoro, H. N. E., Rahajeng, N., Lusiyanti, Y., Rahardjo, T., Erawati, D., Choridah, L., Dhamiyati, W., & Dwidanarti, S. R. (2019) · Biodiversitas Journal of Biological Diversity · doi:10.13057/biodiv/d200805 · Cited by 6
DNA repair at the crossroads of tumor immunogenicity and cancer therapy: Harnessing innate and adaptive immune pathways for improved therapeutic outcomes
Liang, Z., Xu, Y., & Li, C. (2025) · DNA repair · doi:10.1016/j.dnarep.2025.103874 · Cited by 5
“Two in one”: A novel DNA cascade amplification strategy for trace detection of dual targets
Cai, Q., Wang, Y., Ning, Y., & Jie, G. (2024) · Talanta · doi:10.1016/j.talanta.2024.125978 · Cited by 5
Human NEIL1 DNA glycosylase: Structure, function and polymorphisms
Singh, P. K., & Mistry, K. N. (2016) · Meta Gene · doi:10.1016/j.mgene.2016.11.006 · Cited by 5
Two polymorphic mutations in promoter region of DNA polymerase β in relatively higher percentage of thymic hyperplasia patients
Wu, Q., Zhou, S., Liu, J., Tong, H., Sun, Y., Tian, W., Yu, H., Huang, C., Li, D., Jiao, P., et al. (2020) · Thoracic Cancer · doi:10.1111/1759-7714.13773 · Cited by 5
Molecular radiobiology and the origins of the base excision repair pathway: an historical perspective
Wallace, S. S. (2021) · International Journal of Radiation Biology · doi:10.1080/09553002.2021.1908639 · Cited by 5
Self-citation
Development of a Gene Risk Signature for Patients of Pancreatic Cancer
Liu, T., Chen, L., Gao, G., Liang, X., Peng, J., Zheng, M., Li, J., Ye, Y., & Shao, C. (2022) · Journal of Healthcare Engineering · doi:10.1155/2022/4136825 · Cited by 5
Genome-wide analysis of expression quantitative trait loci identified potential lung cancer susceptibility variants among Asian populations
Fan, J., Zhu, M., Wang, Y., Li, Z., Zhang, J., Wang, L., Sun, Q., Dai, J., Jin, G., Hu, Z., et al. (2018) · Carcinogenesis · doi:10.1093/carcin/bgy165 · Cited by 5
[ 18 O]‐Peroxides: Synthesis and Biological Applications
Mascio, P. D., Miyamoto, S., de Medeiros, M. H. G., Martinez, G. R., & Cadet, J. (2014) · Patai's chemistry of functional groups · doi:10.1002/9780470682531.pat0868 · Cited by 5
The Link Between Human Alkyladenine DNA Glycosylase and Cancer Development
Kladova, O. A., & Кузнецова, А. А. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26157647 · Cited by 5
Targeting Base Excision Repair Glycosylases with DNA Containing Transition State Mimics Prepared via Click Chemistry
Yuen, P. K., Green, S. A., Ashby, J., Lay, K. T., Santra, A., Chen, X., Horvath, M. P., & David, S. S. (2018) · ACS Chemical Biology · doi:10.1021/acschembio.8b00771 · Cited by 4
Repair pathway coordination from gap filling by polβ and subsequent nick sealing by LIG1 or LIG3α governs BER efficiency at the downstream steps
Çağlayan, M. (2025) · DNA repair · doi:10.1016/j.dnarep.2025.103826 · Cited by 5
Interplay Between the Cytoskeleton and DNA Damage Response in Cancer Progression
Halim, C. E., Deng, S., Crasta, K., & Yap, C. T. (2025) · Cancers · doi:10.3390/cancers17081378 · Cited by 6
Consequences and repair of radiation-induced DNA damage: fifty years of fun questions and answers
Wallace, S. S. (2021) · International Journal of Radiation Biology · doi:10.1080/09553002.2021.1948141 · Cited by 4
Self-citation
Programmed cell death 4 in bacterially-challenged Apostichopus japonicus: Molecular cloning, expression analysis and functional characterization
Lv, Z., Li, C., Shao, Y., Zhang, W., Wang, Z., & Wang, H. (2016) · Molecular Immunology · doi:10.1016/j.molimm.2016.05.013 · Cited by 4
Nucleus and Genome: DNA Recombination and Repair
Schröpfer, S., Knoll, A., Trapp, O., & Puchta, H. (2014) · Springer eBooks · doi:10.1007/978-1-4939-0263-7_2-1 · Cited by 4
Advanced nano-delivery systems in H. pylori eradication: targeting, efficacy, and clinical translation
Khan, T. U., Sharaf, M., Khan, S., Ahmad, K., & Liu, C. (2025) · Expert Opinion on Drug Delivery · doi:10.1080/17425247.2025.2569642 · Cited by 3
Implications of DNA damage response and immunotherapy in tumor therapy
Li, W., Li, B., Cai, C., Chen, J., Li, Y., Liang, R., & Zhao, Y. (2025) · Cell Communication and Signaling · doi:10.1186/s12964-025-02527-y · Cited by 3
Enhanced Expression of CNTD2/CCNP Predicts Poor Prognosis in Bladder Cancer Based on the GSE13507
Gong, M., Song, E., Huang, G., Ni, W., Dong, W., & Yuan, R. (2021) · Frontiers in Genetics · doi:10.3389/fgene.2021.579900 · Cited by 3
Mouse Embryonic Fibroblasts Isolated From Nthl1 D227Y Knockin Mice Exhibit Defective DNA Repair and Increased Genome Instability
Marsden, C. G., Das, L., Nottoli, T., Kathe, S. D., Doublié, S., Wallace, S. S., & Sweasy, J. B. (2021) · DNA repair · doi:10.1016/j.dnarep.2021.103247 · Cited by 3
Self-citation
Enhanced Sampling for Conformational Changes and Molecular Mechanisms of Human NTHL1
Odstrcil, R. E., Dutta, P., & Liu, J. (2024) · The Journal of Physical Chemistry Letters · doi:10.1021/acs.jpclett.4c00161 · Cited by 3
Impact of DNA ligase inhibition on the nick sealing of polβ nucleotide insertion products at the downstream steps of base excision repair pathway
Almohdar, D., Kamble, P., Basavannacharya, C., Gulkis, M., Calbay, O., Huang, S., Narayan, S., & Çağlayan, M. (2024) · Mutagenesis · doi:10.1093/mutage/geae013 · Cited by 3
Integrating next-generation sequencing and artificial intelligence for the identification and validation of pathogenic variants in colorectal cancer
Rodriguez-Salamanca, J., Angulo-Aguado, M., Orjuela-Amarillo, S., Duque, C., Sierra-Díaz, D. C., Bravo, N. C. C., Figueroa, C., Restrepo, C. M., López‐Cortés, A., Cabrera, R., et al. (2025) · Frontiers in Oncology · doi:10.3389/fonc.2025.1568205 · Cited by 3
Genetic Variant XRCC1 rs1799782 (C194T) and Risk of Cancer Susceptibility in Indian Population: A Meta-analysis of Case–Control Studies
Mandal, R. K., & Mittal, R. D. (2020) · Indian Journal of Clinical Biochemistry · doi:10.1007/s12291-020-00877-7 · Cited by 3
NTHL1 Tumor Syndrome
Kuiper, R. P., Nielsen, M., de Voer, R. M., & Hoogerbrugge, N. (2020) · Europe PMC (PubMed Central) · Cited by 4
Benign Tumors Associated With Heterozygous NTHL1 Variant
Anderson, D. J., Boyle, A., Reinicke, T., Woods, B., & Hsieh, P. C. (2021) · Cureus · doi:10.7759/cureus.16220 · Cited by 3
The hematopoietic compartment is sufficient for lupus development resulting from the POLB-Y265C mutation
Rahim, T., Levinson, M., Carufe, K. E. W., Burak, M. J., Meas, R., Maher, S. E., Bothwell, A. L. M., Gades, N. M., & Sweasy, J. B. (2022) · PLoS ONE · doi:10.1371/journal.pone.0267913 · Cited by 3
Self-citation
Development of a prognostic model for children with neuroblastoma based on necroptosis-related genes
Chu, J. (2022) · Frontiers in Genetics · doi:10.3389/fgene.2022.947000 · Cited by 3
The effect of oral bacterial infection on DNA damage response in host cells.
Oh, J., & Kim, H. (2023) · PubMed Central · Cited by 7
Conformational Dynamics of Biopolymers in the Course of Their Interaction: Multifaceted Approaches to the Analysis by the Stopped-Flow Technique with Fluorescence Detection
Kuznetsov, N. A. (2023) · Photonics · doi:10.3390/photonics10091033 · Cited by 3
Assessing the Phenotype of a Homologous Recombination Deficiency Using High Resolution Array-Based Comparative Genome Hybridization in Ovarian Cancer
Magadeeva, S., Qian, X., Korff, N., Flörkemeier, I., Hedemann, N., Rogmans, C., Förster, M., Arnold, N., Maass, N., Bauerschlag, D., et al. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242417467 · Cited by 3
The Shu complex is an ATPase that regulates Rad51 filaments during homologous recombination in the DNA damage response
Chu, S. S. H., Xing, G., Jha, V., & Ling, H. (2024) · DNA repair · doi:10.1016/j.dnarep.2024.103792 · Cited by 3
The Domino Effect: Nucleosome Dynamics and the Regulation of Base Excision Repair Enzymes
Cook, J. C., & Delaney, S. (2022) · DNA · doi:10.3390/dna2040018 · Cited by 3
Molecular Epidemiology in Amerindians of the Brazilian Amazon Reveals New Genetic Variants in DNA Repair Genes
Cohen-Paes, A. D. N., de Alcântara, A. L., Moreira, F., Fernandes, M. R., Pantoja, K. B. C. C., de Carvalho, D. C., Guerreiro, J., Ribeiro-dos-Santos, Â., dos Santos, S. E. B., de Assumpção, P. P., et al. (2022) · Genes · doi:10.3390/genes13101869 · Cited by 3
Collapsed State Mediates the Low Fidelity of the DNA Polymerase β I260 Mutant
Fijen, C., Chavira, C., Alnajjar, K. S., Sawyer, D. L., & Sweasy, J. B. (2024) · Biochemistry · doi:10.1021/acs.biochem.4c00263 · Cited by 2
Self-citation
The Double Face of Base Excision Repair: Preventing and Triggering Double‐Strand Breaks
Gasser, S. M. (2025) · BioEssays · doi:10.1002/bies.70092 · Cited by 2
Linker-mediated conformational coupling drives lesion recognition in MutY glycosylase
Kim, H., Lim, M., & Pak, Y. (2026) · Nucleic Acids Research · doi:10.1093/nar/gkag483 · Cited by 2
The DNA damage response and cancer immunotherapy
Sheng, H., & Li, G. (2026) · Nature reviews. Cancer · doi:10.1038/s41568-026-00958-4 · Cited by 3
A Novel Hypoxia-related lncRNA Risk Score Model for Prognosis Evaluation of Clear Cell Renal Cell Carcinoma
Fu, L., Li, X., Zhou, X., Tong, H., Hu, Z., Bai, X., & Gou, X. (2023) · Combinatorial Chemistry & High Throughput Screening · doi:10.2174/1386207326666230606152615 · Cited by 2
Impact of polβ/XRCC1 Interaction Variants on the Efficiency of Nick Sealing by DNA Ligase IIIα in the Base Excision Repair Pathway
Almohdar, D., Gulkis, M., Ortiz, A., Tang, Q., Sobol, R. W., & Çağlayan, M. (2023) · Journal of Molecular Biology · doi:10.1016/j.jmb.2023.168410 · Cited by 2
Epigenetic orchestration of the DNA damage response: Insights into the regulatory mechanisms
Mondal, A., Sarkar, A., Das, D., Sengupta, A., Kabiraj, A., Mondal, P., Nag, R., Mukherjee, S., & Das, C. (2024) · International review of cytology · doi:10.1016/bs.ircmb.2024.03.003 · Cited by 3
Interaction of base excision repair gene polymorphism and estrogen-DNA adducts in breast cancer risk among East Asian women
Chen, H.-W., Kuo, W., Lu, Y., Chen, I.-C., Hu, F., Wang, M.-Y., Zahid, M., Rogan, E. G., Cheng, A., & Lin, C. (2024) · Breast Cancer Research and Treatment · doi:10.1007/s10549-024-07418-3 · Cited by 2
APEX1 Polymorphisms Affect Acute Myeloid Leukemia Risk, and Its Expression Is Involved in Cell Proliferation and Differentiation
Gotoh, N., Oda, T., Kitamura, Y., Shiraishi, N., Aoyagi, R., Omori, A., Yanagisawa, K., Iida, M., Itoi, Y., Negishi, H., et al. (2024) · International Journal of Laboratory Hematology · doi:10.1111/ijlh.14401 · Cited by 2
Active DNA Demethylation in Development, Human Disease, and Cancer
Tricarico, R., & Bellacosa, A. (2016) · Springer eBooks · doi:10.1007/978-4-431-55873-6_21 · Cited by 2
Comparative Analysis of the Activity of the Polymorphic Variants of Human Uracil-DNA-Glycosylases SMUG1 and MBD4
Alekseeva, I. V., Bakman, A. S., Iakovlev, D. A., Kuznetsov, N. A., & Fedorova, O. S. (2021) · Molecular Biology · doi:10.1134/s0026893321020035 · Cited by 2
Inhibition of Human APE1 and MTH1 DNA Repair Proteins by Dextran-Coated γ-Fe 2 O 3 Ultrasmall Superparamagnetic Iron Oxide Nanoparticles
Coşkun, E., Singh, N., Scanlan, L. D., Jaruga, P., Doak, S. H., Dizdaroğlu, M., & Nelson, B. C. (2022) · Nanomedicine · doi:10.2217/nnm-2022-0204 · Cited by 2
[Genetic Mutation Screening of DNA Polymerase in Human Lung Cancer].
Wu, Q., Tian, W., Yu, H., Huang, C., Jiao, P., Ma, C., Wang, Y., Huang, W., Sun, Y., Ai, B., et al. (2019) · Europe PMC (PubMed Central) · doi:10.3779/j.issn.1009-3419.2019.07.04 · Cited by 2
Long Non-coding RNAs and Cancer Cells’ Drug Resistance: An Unexpected Connection
Pucci, P., Yuen, W., Venalainen, E., Roig-Carles, D., Wang, Y. Z., & Crea, F. (2020) · RNA technologies · doi:10.1007/978-3-030-44743-4_7 · Cited by 2
The impact of rare germline variants on human somatic mutation processesPreprint
Vali-Pour, M., Lehner, B., & Supek, F. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.11.14.468508 · Cited by 2
GASTROINTESTINAL CANCER SYNDROMES
Schneider, K. A., Chittenden, A. B., & Shannon, K. (2023) · doi:10.1002/9781119466499.ch2 · Cited by 2
Base Excision Repair: A Review
Sidhu, A. (2023) · Journal of BioMed Research and Reports · doi:10.59657/2837-4681.brs.23.032 · Cited by 1
Dna Glycosylases Remove Oxidized Base Damages From G-Quadruplex Dna Structures
Zhou, J. (2015) · ScholarWorks -A service of University of Vermont Libraries (University of Vermont) · Cited by 1
Illuminating the route of precision medicine and inhibitor discovery: real-time measurement of DNA repair capacity with molecular beacons
Bellacosa, A., & Yen, T. J. (2018) · Oncotarget · doi:10.18632/oncotarget.26056 · Cited by 1
Signal-on/signal-off bead-based assays for the multiplexed monitoring of base excision repair activities by flow cytometry
Gines, G., Brusa, C., Saint‐Pierre, C., & Gasparutto, D. (2022) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-021-03849-9 · Cited by 1
Associations of DNA Base Excision Repair and Antioxidant Enzyme Genetic Risk Scores with Biomarker of Systemic Inflammation
Mao, Z., Gray, A. L. H., Gross, M. D., Thyagarajan, B., & Bostick, R. M. (2022) · Frontiers in Aging · doi:10.3389/fragi.2022.897907 · Cited by 1
Transgenic mice harboring direct repeat substrates reveal key underlying causes of homologous recombination in vivo
Moise, A. C., Kay, J. E., & Engelward, B. P. (2022) · DNA repair · doi:10.1016/j.dnarep.2022.103419 · Cited by 1
β-Like DNA polymerases and prospects for their use as targets in chemotherapy of tumors
Davydov, V. V., Bukhvostov, A. A., & Kuznetsov, D. A. (2023) · Biomeditsinskaya Khimiya · doi:10.18097/pbmc20236903145 · Cited by 1
Highly Sensitive Radioactivity-Based DNA 3′-Phosphatase Activity Assay for Polynucleotide Kinase 3′-Phosphatase
Chakraborty, A., & Hazra, T. K. (2023) · Methods in molecular biology · doi:10.1007/978-1-0716-3373-1_3 · Cited by 1
Enhanced glutathione levels confer resistance to apoptotic and ferroptotic programmed cell death in NEIL DNA glycosylase deficient HAP1 cells
Neurauter, C. G., Pannone, M., de Sousa, M. M. L., Wang, W., Kuśnierczyk, A., Luna, L., Sætrom, P., Scheffler, K., & Bjørås, M. (2024) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2024.01.037 · Cited by 1
Thermostability and excision activity of polymorphic forms of hOGG1
Mouzakis, K. D., Wu, T. C., & Haushalter, K. A. (2019) · BMC Research Notes · doi:10.1186/s13104-019-4111-9 · Cited by 1
The double-edged sword of cancer mutations: exploiting neoepitopes for the fight against cancer
Alvarado-Cruz, I., Meas, R., Paluri, S. L. A., Carufe, K. E. W., Khan, M., & Sweasy, J. B. (2019) · Mutagenesis · doi:10.1093/mutage/gez049 · Cited by 1
Self-citation
Link between Base Excision Repair (BER), Reactive Oxygen Species (ROS), and Cancer
Fayyad, N., Kobaisi, F., Fayyad‐Kazan, M., Nasrallah, A., Fayyad‐Kazan, H., & Rachidi, W. (2021) · Vide Leaf, Hyderabad eBooks · doi:10.37247/imcac.1.2021.8 · Cited by 1
Crystal structure of the apurinic/apyrimidinic endonuclease XthA (HP1526 protein) from Helicobacter pylori
Dinh, T., Dao, O., Asaithambi, K., Ngo, D., & Lee, K. H. (2023) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2023.04.047 · Cited by 1
DNA Damage Response Pathways in Cancer Predisposition and Progression
Ashour, M. E., El-Shafie, L., & El‐Khamisy, S. F. (2014) · Cancer metastasis · doi:10.1007/978-3-319-12136-9_3
Biochemical characterization of mammalian NEIL3 and involvement in repair of hydantoin lesions in proliferative tissue.
Krokeide, S. Z. (2013) · NORA - Norwegian Open Research Archives
Analysis of the Genetic Requirements for Rad51-Mediated 3’ Polymerization during DNA Repair by Homologous Recombination
Mundia, M. M. (2016) · The Atrium (University of Guelph)
In Vivo DNA Repair Mechanisms and Carcinogenesis
Woodrick, J. (2014) · ProQuest Demo Repository
Mechanisms and Dynamics of Oxidative DNA Damage Repair in Nucleosomes
Cannan, W. J. (2016) · ScholarWorks -A service of University of Vermont Libraries (University of Vermont) · doi:10.13140/rg.2.2.10290.20165
Targeting ATR for Cancer Therapy: Profile and Expectations for ATR Inhibitors
Curtin, N. J., & Pollard, J. R. (2018) · Cancer drug discovery and develogment/Cancer drug discovery and development · doi:10.1007/978-3-319-75836-7_4
Molecular Mechanisms of Activation Induced Deaminase Specificity
Prado, Á. F. Á. (2018) · doi:10.4321/repisalud.6447
Trinucleotide Repeat Instability Modulated by DNA Repair Enzymes and Cofactors
Ren, Y. (2018) · FIU - Digital Commons (Florida International University) · doi:10.25148/etd.fidc006873
Modelling the impact of cellular variation on flux through base excision DNA repair.
Healing, E. (2019) · Surrey Research Insight Open Access (The University of Surrey) · doi:10.15126/thesis.00850299
RECQL4; Linking DNA Replication and Bone Tumourigenesis
Author, U. (2019) · Lincoln Repository (University of Lincoln) · doi:10.24385/lincoln.24326188
The role of receptor tyrosine kinases in mediating glioblastoma resistance to radiotherapy and temozolomide
Areeb, Z. (2020) · Minerva Access (University of Melbourne)
Excision of mutagenic replication-blocking lesions suppresses cancer but promotes cytotoxicity and lethality in nitrosamine-exposed micePreprint
Kay, J. E., Corrigan, J. J., Armijo, A. L., Nazari, I. S., Kohale, I. N., Torous, D. K., Avlasevich, S. L., Croy, R. G., Wadduwage, D. N., Carrasco, S. E., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.01.12.426356
Characterizing the Genome-wide Associations of Somatic Mutations and Chromatin Accessibility in Cancer
Ocsenas, O. (2020) · TSpace (University of Toronto)
Evolución de la genómica tumoral
Cardona, A. F., Arrieta, O. G., Zatarain-Barron, Z. L., Rolfo, C. D., Ordóñez‐Reyes, C., & Patiño, A. R. (2021) · Medicina · doi:10.56050/01205498.1566
Versatile cell-based assay for measuring DNA alkylation damage and its repairPreprint
Li, Y., Mao, P., Basenko, E. Y., Lewis, Z., Smerdon, M. J., & Czaja, W. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.02.25.432902
Association of polymorphisms in FLT3, EGFR, ALOX5, and NEIL3 with glioblastoma in the Han Chinese population
JinXiao-Lan, T.-B., & Yang, L. (2013)
Forecasting the Reaction of DNA Modifying Enzymes on DNA Nanostructures by Coarse Grained Model for Stimuli-Responsive Drug DeliveryPreprint
Deng, Y., Tan, Y., Zhang, L., Zhang, C., & Su, X. (2021) · Research Square · doi:10.21203/rs.3.rs-1038517/v1
Hypoxia-related lncRNA Signature to Predict the Survival of Patients with Clear Cell Renal Cell CarcinomaPreprint
Fu, L., Li, X., Zhou, X., Tong, H., & Gou, X. (2022) · Research Square · doi:10.21203/rs.3.rs-1178273/v1
Multidrug resistance, a major obstacle in hepatocellular carcinoma treatment: challenges and future perspectives
Sahu, T. A., Mehta, A., Verma, H. K., & Bhaskar, L. V. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-98807-0.00020-x

Authors: Wallace, S. S., Murphy, D. L., & Sweasy, J. B.
Affiliations: University of Vermont (US)
Yale University (US)
Corresponding author: Wallace, Susan S.
ORCID: Wallace, Susan S.
Sweasy, Joann B.
Venue: Cancer Letters
Publisher: Elsevier BV
Published: 2012-12
Volume: 327
Issue: 1-2
Pages: 73-89
ISSN: 0304-3835 (ISSN-L)
DOI: 10.1016/j.canlet.2011.12.038
PMC: PMC3361536
OpenAlex: W1985323804
Cited by: 329
References: 357
Citations by year: 2026: 17 · 2025: 21 · 2024: 17 · 2023: 32 · 2022: 34 · 2021: 34 · 2020: 26 · 2019: 27 · 2018: 26 · 2017: 15 · 2016: 23 · 2015: 14 · 2014: 25 · 2013: 16 · 2012: 2
FWCI: 1.66
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Cancer Letters (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
Funders: National Cancer Institute (P01CA098993, R01CA080830, R01 CA33657, P01CA129186, R01CA033657)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
Health Sciences › Medicine › Pathology and Forensic Medicine › Genetic factors in colorectal cancer
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Carcinogens and Genotoxicity Assessment
Keywords: base excision repair, short-patch repair, DNA repair deficiency, cancer susceptibility, MUTYH, biallelic variants, mouse model, endogenous DNA damage, neurological disorders
MeSH terms: Animals, Cell Transformation, Neoplastic, DNA Damage, DNA Repair, Humans, Neoplasms, Phenotype, Gene Expression Regulation, Neoplastic, Genetic Predisposition to Disease, DNA Repair Enzymes

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Base excision repair and cancer

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks