The DOI matches its Crossref record; 11 of the 11 references it cites were found in a registry or an index.
Detection of Topoisomerase Covalent Complexes in Eukaryotic Cells
Abstract
DNA topoisomerases carry out topological transformations of DNA by introducing transient DNA breaks. The covalent intermediate of topoisomerase reactions include the topoisomerase protein covalently bound to DNA by a phosphotyrosine intermediate. Anti-cancer drugs that target topoisomerases typically trap the covalent intermediate, and generate cytotoxic enzyme dependent DNA damage. More recently, structural alterations in DNA such as DNA damage have also been shown to trap covalent intermediates of topoisomerase reactions. Understanding the action of drugs that target topoisomerases as well as determining the importance of trapped topoisomerases on genome stability requires assays that can accurately and sensitively measure levels of topoisomerase/DNA complexes. This chapter describes two approaches that have been developed to quantitate topoisomerase DNA complexes. These assays termed ICE (in vivo complex of enzymes) and RADAR (rapid approach to DNA adduct recovery) rely on isolation of genomic DNA under conditions that preserve proteins covalently bound to DNA. Covalently bound proteins are then quantitated using antibodies directed against specific topoisomerases. We describe assays in both mammalian cells and the yeast Saccharomyces cerevisiae that can measure topoisomerase/DNA covalent complexes, and give examples that can be used to enhance the quantitative reliability of these assays.
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“Doxorubicin (DOX) is one of the most effective chemotherapeutical components for treating various types of cancer (Anand et al., 2018; Menendez et al., 2022).”
From pH stimuli-responsive hydrogels from non-cellulosic biopolymers for drug delivery. (2023) · cites this paper as Anand et al., 2018
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Cites
Roles of eukaryotic topoisomerases in transcription, replication and genomic stability
Pommier, Y. G., Sun, Y., Huang, S.-Y. N., & Nitiss, J. L. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.111 · Cited by 989
Self-citationDrugging Topoisomerases: Lessons and Challenges
Pommier, Y. G. (2012) · ACS Chemical Biology · doi:10.1021/cb300648v · Cited by 867
All tangled up: how cells direct, manage and exploit topoisomerase function
Vos, S. M., Tretter, E. M., Thurtle-Schmidt, B. H., & Berger, J. M. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3228 · Cited by 681
The DNA cleavage reaction of topoisomerase II: wolf in sheep's clothing
Deweese, J. E., & Osheroff, N. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkn937 · Cited by 466
New Mechanistic and Functional Insights into DNA Topoisomerases
Chen, S. H., Chan, N., & Hsieh, T. (2013) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061809-100002 · Cited by 370
DNA Topoisomerase II as a Target for Cancer Chemotherapy
Walker, J. V., & Nitiss, J. L. (2002) · Cancer Investigation · doi:10.1081/cnv-120002156 · Cited by 138
Self-citationA rapid and sensitive assay for DNA–protein covalent complexes in living cells
Kiianitsa, K., & Maizels, N. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt171 · Cited by 128
Subramanian, D., Rosenstein, B. S., & Muller, M. T. (1998) · PubMed · Cited by 83
Kiianitsa, K., & Maizels, N. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku490 · Cited by 38
Using Yeast to Understand Drugs that Target Topoisomerasesa
Nitiss, J. L., Rose, A., Sykes, K. C., HARRIS, J., & Zhou, J. (1996) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1996.tb26374.x · Cited by 33
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Research works printed but not linked: 2
- Nitiss JL, Soans E, Rogojina A, Seth A, Mishina M (2012) Topoisomerase assays. Curr Protoc Pharmacol Chapter 3:Unit 3 3
- Nitiss JL (2001) Topoisomerase assays. Curr Protoc Pharmacol Chapter 3:Unit3 3
Cited by
pH stimuli-responsive hydrogels from non-cellulosic biopolymers for drug delivery.
Vegad, U., Patel, M., Khunt, D., Zupančič, O., Chauhan, S., & Paudel, A. (2023) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2023.1270364 · Cited by 85
“Doxorubicin (DOX) is one of the most effective chemotherapeutical components for treating various types of cancer (Anand et al., 2018; Menendez et al., 2022).”
BackgroundMenendez, D., Anand, J. R., Murphy, C. C., Bell, W. J., Fu, J., Slepushkina, N., Buehler, E., Martin, S. E., Lal-Nag, M., Nitiss, J. L., et al. (2022) · Oncotarget · doi:10.18632/oncotarget.28195 · Cited by 22
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Metadata
- Authors
- Anand, J., Sun, Y., Zhao, Y., Nitiss, K. C., & Nitiss, J. L.
- Affiliations
- University of Illinois Chicago, Rockford campus (US)
- Corresponding author
- Nitiss, John L.
- Venue
- Methods in molecular biology
- Publisher
- Springer New York
- Published
- 2017-11-25
- Volume
- 1703
- Pages
- 283-299
- ISSN
- 1064-3745 (ISSN-L)
- 1940-6029
- OpenAlex
- W2768589370
- Cited by
- 31
- References
- 11
- Citations by year
- 2026: 1 · 2025: 3 · 2023: 5 · 2022: 9 · 2021: 4 · 2020: 8 · 2017: 1
- FWCI
- 3.07
- Type
- book chapter
- Language
- en
- Open access
- closed
- Locations
- Methods in molecular biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Cancer Institute (R03CA216010)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cancer therapeutics and mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA and Nucleic Acid Chemistry
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Toxicology › Bioactive Compounds and Antitumor Agents
- Keywords
- DNA topoisomerase, topoisomerase inhibitors, anticancer agents, DNA damage, genome stability, Saccharomyces cerevisiae, mammalian cells
- MeSH terms
- Animals, DNA, DNA Topoisomerases, Type I, Humans, Mammals, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins
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- Anand, J., Sun, Y., Zhao, Y., Nitiss, K. C., & Nitiss, J. L. (2018). Detection of Topoisomerase Covalent Complexes in Eukaryotic Cells. Methods in molecular biology. https://doi.org/10.1007/978-1-4939-7459-7_20
