ArticleThe EMBO journal2006
Structure of the N-terminal fragment of topoisomerase V reveals a new family of topoisomerases.
Article in The EMBO journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
33 citing papers in PubMed, 54 citations in OpenAlex.
- The Roles of Topoisomerases in Transcriptional Regulation.International journal of molecular sciences · 2026Review
- Structural insights into the assembly of type IIA topoisomerase DNA cleavage-religation center.Nucleic acids research · 2024Article
- Stability Islands and the Folding Cooperativity of a Seven-Repeat Array from Topoisomerase V.Journal of the American Chemical Society · 2023Article
- Article
- A tale of topoisomerases and the knotty genetic material in the backdrop of Plasmodium biology.Bioscience reports · 2022Review
- DNA topoisomerases: Advances in understanding of cellular roles and multi-protein complexes via structure-function analysis.BioEssays : news and reviews in molecular, cellular and developmental biology · 2021Review
- Archaea: A Gold Mine for Topoisomerase Diversity.Frontiers in microbiology · 2021Review
- DNA topoisomerases as molecular targets for anticancer drugs.Journal of enzyme inhibition and medicinal chemistry · 2020Review
- Probing structural requirements for human topoisomerase I inhibition by a novel N1-Biphenyl fluoroquinolone.European journal of medicinal chemistry · 2019Article
- Topoisomerases as anticancer targets.The Biochemical journal · 2018Review
- Methanopyrus kandleri topoisomerase V contains three distinct AP lyase active sites in addition to the topoisomerase active site.Nucleic acids research · 2016Article
- In Situ Proteolysis for Crystallization of Membrane Bound Cytochrome P450 17A1 and 17A2 Proteins from Zebrafish.Current protocols in protein science · 2016Article
- Article
- DNA Topoisomerases.EcoSal Plus · 2015Review
- Biochemical characterization of the topoisomerase domain of Methanopyrus kandleri topoisomerase V.The Journal of biological chemistry · 2014Article
- Chromatin structure and dynamics in hot environments: architectural proteins and DNA topoisomerases of thermophilic archaea.International journal of molecular sciences · 2014Review
- DNA topoisomerase VIII: a novel subfamily of type IIB topoisomerases encoded by free or integrated plasmids in Archaea and Bacteria.Nucleic acids research · 2014Article
- Article
- Identification of one of the apurinic/apyrimidinic lyase active sites of topoisomerase V by structural and functional studies.Nucleic acids research · 2013Article
- Remote control of DNA-acting enzymes by varying the Brownian dynamics of a distant DNA end.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Topoisomerases are involved in controlling and maintaining the topology of DNA and are present in all kingdoms of life. Unlike all other types of topoisomerases, similar type IB enzymes have only been identified in bacteria and eukarya. The only putative type IB topoisomerase in archaea is represented by Methanopyrus kandleri topoisomerase V. Despite several common functional characteristics, topoisomerase V shows no sequence similarity to other members of the same type. The structure of the 61 kDa N-terminal fragment of topoisomerase V reveals no structural similarity to other topoisomerases. Furthermore, the structure of the active site region is different, suggesting no conservation in the cleavage and religation mechanism. Additionally, the active site is buried, indicating the need of a conformational change for activity. The presence of a topoisomerase in archaea with a unique structure suggests the evolution of a separate mechanism to alter DNA.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.