ArticleThe Journal of biological chemistry2017
A helical bundle in the N-terminal domain of the BLM helicase mediates dimer and potentially hexamer formation.
Article in The Journal of biological chemistry, 2017. 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.
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Who cites it
11 citing papers in PubMed, 20 citations in OpenAlex.
- Centromere protection requires strict mitotic inactivation of the Bloom syndrome helicase complex.Nature communications · 2025Article
- Article
- The convergence of head-on DNA unwinding forks induces helicase oligomerization and activity transition.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Bloom helicase mediates formation of large single-stranded DNA loops during DNA end processing.Nature communications · 2022Article
- Mechanism of Bloom syndrome complex assembly required for double Holliday junction dissolution and genome stability.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- The toposiomerase IIIalpha-RMI1-RMI2 complex orients human Bloom's syndrome helicase for efficient disruption of D-loops.Nature communications · 2022Article
- The Bloom syndrome complex senses RPA-coated single-stranded DNA to restart stalled replication forks.Nature communications · 2021Article
- Human RecQ Helicases in DNA Double-Strand Break Repair.Frontiers in cell and developmental biology · 2021Review
- RecQ helicases in DNA repair and cancer targets.Essays in biochemistry · 2020Review
- Article
- Construction, expression, and characterization of AG1Data in brief · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Helicases play a critical role in processes such as replication or recombination by unwinding double-stranded DNA; mutations of these genes can therefore have devastating biological consequences. In humans, mutations in genes of three members of the RecQ family helicases (
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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.