ReviewInternational journal of molecular sciences2017
Non-Catalytic Roles of the Topoisomerase IIα C-Terminal Domain.
Review in International journal of molecular sciences, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 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
21 citing papers in PubMed, 28 citations in OpenAlex.
- Type II topoisomerase substrate geometry revealed through combined experiment and computation.bioRxiv : the preprint server for biology · 2026Article
- Adaptive evolution of Topoisomerase II triggers reproductive isolation in Drosophila.bioRxiv : the preprint server for biology · 2026Article
- Histone H3 N-Terminal Tail Residues Important for Meiosis inBiomolecules · 2025Article
- Mitotic genome folding.The Journal of cell biology · 2025Review
- Mutagenesis of Intrinsically Disordered Domain Impacts Topoisomerase IIα Catalytic Activity.International journal of molecular sciences · 2025Article
- Histone H3 tail modifications required for meiosis inbioRxiv : the preprint server for biology · 2024Article
- Structural and functional insights into the T-even type bacteriophage topoisomerase II.Nature communications · 2024Article
- Bioinformatic Analysis of Topoisomerase IIα Reveals Interdomain Interdependencies and Critical C-Terminal Domain Residues.International journal of molecular sciences · 2024Article
- Aspergillus SUMOylation mutants exhibit chromosome segregation defects including chromatin bridges.Genetics · 2023Article
- Structural basis for allosteric regulation of Human Topoisomerase IIα.Nature communications · 2021Article
- Histone H2A phosphorylation recruits topoisomerase IIα to centromeres to safeguard genomic stability.The EMBO journal · 2020Article
- Telomere fusions and translocations: a bridge too far?Current opinion in genetics & development · 2020Review
- The interplay between DNA topoisomerase 2α post-translational modifications and drug resistance.Cancer drug resistance (Alhambra, Calif.) · 2020Review
- PICH and TOP3A cooperate to induce positive DNA supercoiling.Nature structural & molecular biology · 2019Article
- The Impact of the C-Terminal Region on the Interaction of Topoisomerase II Alpha with Mitotic Chromatin.International journal of molecular sciences · 2019Article
- Casein kinase II-dependent phosphorylation of DNA topoisomerase II suppresses the effect of a catalytic topo II inhibitor, ICRF-193, in fission yeast.The Journal of biological chemistry · 2019Article
- SUMO-Mediated Regulation of Nuclear Functions and Signaling Processes.Molecular cell · 2018Review
- The Roles of DNA Topoisomerase IIβ in Transcription.International journal of molecular sciences · 2018Review
- Site-Specific Cleavage by Topoisomerase 2: A Mark of the Core Centromere.International journal of molecular sciences · 2018Article
- A Topology-Centric View on Mitotic Chromosome Architecture.International journal of molecular sciences · 2017Review
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
DNA Topoisomerase IIα (Topo IIα) is a ubiquitous enzyme in eukaryotes that performs the strand passage reaction where a double helix of DNA is passed through a second double helix. This unique reaction is critical for numerous cellular processes. However, the enzyme also possesses a C-terminal domain (CTD) that is largely dispensable for the strand passage reaction but is nevertheless important for the fidelity of cell division. Recent studies have expanded our understanding of the roles of the Topo IIα CTD, in particular in mitotic mechanisms where the CTD is modified by Small Ubiquitin-like Modifier (SUMO), which in turn provides binding sites for key regulators of mitosis.
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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.