ReviewCells2024
Variation of Structure and Cellular Functions of Type IA Topoisomerases across the Tree of Life.
Review in Cells, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
11 citing papers in PubMed, 14 citations in OpenAlex.
- New Insights into Binding of G-segment DNA to the Active Site of Escherichia coli Topoisomerase III.Scientific reports · 2026Article
- Coordinated topoisomerase function shapes the fluoroquinolone response ofbioRxiv : the preprint server for biology · 2026Article
- Search for Specific Inhibitors Targeting Type IA Topoisomerases.Journal of molecular biology · 2026Review
- Investigation of potential hinge region forbioRxiv : the preprint server for biology · 2026Article
- The SWIB domain-containing DNA topoisomerase I ofJournal of bacteriology · 2025Article
- Substituted Triazole-3,5-Diamine Compounds as Novel Human Topoisomerase III Beta Inhibitors.International journal of molecular sciences · 2025Article
- Deciphering the human TopIIIα activity modulated by Rmi1 using magnetic tweezers.Nucleic acids research · 2025Article
- Regulation of DNA Topology in Archaea: State of the Art and Perspectives.Molecular microbiology · 2025Review
- Bacterial Topoisomerase I Growth Complementation Assay.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Temporospatial control of topoisomerases by essential cellular processes.Current opinion in microbiology · 2024Review
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
Topoisomerases regulate the topological state of cellular genomes to prevent impediments to vital cellular processes, including replication and transcription from suboptimal supercoiling of double-stranded DNA, and to untangle topological barriers generated as replication or recombination intermediates. The subfamily of type IA topoisomerases are the only topoisomerases that can alter the interlinking of both DNA and RNA. In this article, we provide a review of the mechanisms by which four highly conserved N-terminal protein domains fold into a toroidal structure, enabling cleavage and religation of a single strand of DNA or RNA. We also explore how these conserved domains can be combined with numerous non-conserved protein sequences located in the C-terminal domains to form a diverse range of type IA topoisomerases in Archaea, Bacteria, and Eukarya. There is at least one type IA topoisomerase present in nearly every free-living organism. The variation in C-terminal domain sequences and interacting partners such as helicases enable type IA topoisomerases to conduct important cellular functions that require the passage of nucleic acids through the break of a single-strand DNA or RNA that is held by the conserved N-terminal toroidal domains. In addition, this review will exam a range of human genetic disorders that have been linked to the malfunction of type IA topoisomerase.
Indexed as
Identifiers
What OpenQuestion holds
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.