ArticleNature communications2021
Structural basis for allosteric regulation of Human Topoisomerase IIα.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed, 76 citations in OpenAlex.
- Design, synthesis, and anticancer evaluation of a novel imine-linked covalent organic framework correlated to molecular docking and DFT insights.RSC advances · 2026Article
- STUB1 downregulates TOP2A through a dual mechanism of ubiquitination and FOXM1-mediated transcription repression, suppressing breast cancer growth and enhancing sensitivity to chemotherapy.Cellular & molecular biology letters · 2026Article
- MYC modulates TOP2A diffusion to promote substrate detection and activity.Nature communications · 2026Article
- Coumarin-Augmented Thiazole Hybrids as Dual Anticancer and Antibacterial Agents.Chemical biology & drug design · 2026Article
- Direct trapping of the transport-segment DNA by the central domain of type IIA topoisomerases.Science advances · 2025Article
- Mutagenesis of Intrinsically Disordered Domain Impacts Topoisomerase IIα Catalytic Activity.International journal of molecular sciences · 2025Article
- Structural insights into fungal and human topoisomerase II with implications for in silico antifungal drug design.Scientific reports · 2025Article
- Targeting DNA Topoisomerase IIα in Retinoblastoma: Implications in EMT and Therapeutic Strategies.Biologics : targets & therapy · 2025Article
- Structural basis of chiral wrap and T-segment capture byProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Simulation- and AI-directed optimization of 4,6-substituted 1,3,5-triazin-2(1Computational and structural biotechnology journal · 2024Article
- Structural basis for difunctional mechanism of m-AMSA against African swine fever virus pP1192R.Nucleic acids research · 2024Article
- Structural and functional insights into the T-even type bacteriophage topoisomerase II.Nature communications · 2024Article
- Structural insights into the assembly of type IIA topoisomerase DNA cleavage-religation center.Nucleic acids research · 2024Article
- Modeling allosteric mechanisms of eukaryotic type II topoisomerases.Biophysical journal · 2024Article
- Structural insights into the DNA topoisomerase II of the African swine fever virus.Nature communications · 2024Article
- Bioinformatic Analysis of Topoisomerase IIα Reveals Interdomain Interdependencies and Critical C-Terminal Domain Residues.International journal of molecular sciences · 2024Article
- PRRX1-TOP2A interaction is a malignancy-promoting factor in human malignant peripheral nerve sheath tumours.British journal of cancer · 2024Article
- Structural basis of DNA crossover capture byScience (New York, N.Y.) · 2024Article
- Structure-function analysis of the ATPase domain of African swine fever virus topoisomerase.mBio · 2024Article
- 1,2,3-Triazole Hybrids Containing Isatins and Phenolic Moieties: Regioselective Synthesis and Molecular Docking Studies.Molecules (Basel, Switzerland) · 2024Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The human type IIA topoisomerases (Top2) are essential enzymes that regulate DNA topology and chromosome organization. The Topo IIα isoform is a prime target for antineoplastic compounds used in cancer therapy that form ternary cleavage complexes with the DNA. Despite extensive studies, structural information on this large dimeric assembly is limited to the catalytic domains, hindering the exploration of allosteric mechanism governing the enzyme activities and the contribution of its non-conserved C-terminal domain (CTD). Herein we present cryo-EM structures of the entire human Topo IIα nucleoprotein complex in different conformations solved at subnanometer resolutions (3.6-7.4 Å). Our data unveils the molecular determinants that fine tune the allosteric connections between the ATPase domain and the DNA binding/cleavage domain. Strikingly, the reconstruction of the DNA-binding/cleavage domain uncovers a linker leading to the CTD, which plays a critical role in modulating the enzyme's activities and opens perspective for the analysis of post-translational modifications.
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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.