ArticleNucleic acids research2015
Crystal structure of the Bloom's syndrome helicase indicates a role for the HRDC domain in conformational changes.
Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.
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Who cites it
58 citing papers in PubMed, 92 citations in OpenAlex.
- Design, synthesis, and anti-prostate cancer activity evaluation of novel thieno[2,3-b]pyridine derivatives as potential BLM helicase inhibitors.Molecular diversity · 2026Article
- Shuttling of RecQ helicase HIM-6 coordinates iterative cycle of unwinding, pulling, and backsliding.Nucleic acids research · 2026Article
- G-Quadruplex Unwinding Molecular Mechanisms by Helicases and Their Applications.International journal of molecular sciences · 2026Review
- WRN structural flexibility showcased through fragment-based lead discovery of inhibitors.Nature communications · 2026Article
- Using the safety scissors: DNA resection regulation at DNA double-strand breaks and telomeres.DNA repair · 2025Review
- Review
- Efficient coordination between the winged helix domain and the aromatic-rich loop restructures the ATPase domain and facilitates DNA unwinding by human RECQ1.Nucleic acids research · 2025Article
- Biophysical investigation of the molecular interaction between minichromosome maintenance protein 6 and Bloom syndrome helicase.The FEBS journal · 2025Article
- Article
- Multiple functions of the ALT favorite helicase, BLM.Cell & bioscience · 2025Review
- Structural Chemistry of Helicase Inhibition.Journal of medicinal chemistry · 2025Review
- Synergistic effects of bloom helicase (BLM) inhibitor AO/854 with cisplatin in prostate cancer.Scientific reports · 2024Article
- Response to Replication Stress and Maintenance of Genome Stability by WRN, the Werner Syndrome Protein.International journal of molecular sciences · 2024Review
- Article
- Using a Function-First "Scout Fragment"-Based Approach to Develop Allosteric Covalent Inhibitors of Conformationally Dynamic Helicase Mechanoenzymes.Journal of the American Chemical Society · 2024Article
- BLM helicase protein negatively regulates stress granule formation through unwinding RNA G-quadruplex structures.Nucleic acids research · 2023Article
- The MRN complex and topoisomerase IIIa-RMI1/2 synchronize DNA resection motor proteins.The Journal of biological chemistry · 2023Article
- Biochemical Properties of Naturally Occurring Human Bloom Helicase Variants.bioRxiv : the preprint server for biology · 2023Article
- Article
- Biochemical and Structural Analyses Shed Light on the Mechanisms of RadD DNA Binding and Its ATPase fromInternational journal of molecular sciences · 2023Article
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Authors and funding
11 authors at 4 institutions in 3 countries.
Funding
Abstract
Bloom's syndrome helicase (BLM) is a member of the RecQ family of DNA helicases, which play key roles in the maintenance of genome integrity in all organism groups. We describe crystal structures of the BLM helicase domain in complex with DNA and with an antibody fragment, as well as SAXS and domain association studies in solution. We show an unexpected nucleotide-dependent interaction of the core helicase domain with the conserved, poorly characterized HRDC domain. The BLM-DNA complex shows an unusual base-flipping mechanism with unique positioning of the DNA duplex relative to the helicase core domains. Comparison with other crystal structures of RecQ helicases permits the definition of structural transitions underlying ATP-driven helicase action, and the identification of a nucleotide-regulated tunnel that may play a role in interactions with complex DNA substrates.
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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.