ArticleCell2009
Molecular architecture of the Mos1 paired-end complex: the structural basis of DNA transposition in a eukaryote.
Article in Cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 97 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.
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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
97 citing papers in PubMed, 146 citations in OpenAlex.
- Structure-based recasting of a mammalian DNA transpososome as an obligate heterodimer.bioRxiv : the preprint server for biology · 2026Article
- Evidence for dual pathways of Tc1/mariner domestication in Drosophila.BMC biology · 2026Article
- mariner elements as a model for analyzing the stress response and somatic mobilization activity of transposable elements.Heredity · 2025Review
- Relaxed DNA substrate specificity of transposases involved in programmed genome rearrangement.Nucleic acids research · 2025Article
- Transposable Elements Drive Regulatory and Functional Innovation of F-box Genes.Molecular biology and evolution · 2025Article
- Optimized genetic tools for neuroanatomical and functional mapping of the Aedes aegypti olfactory system.G3 (Bethesda, Md.) · 2025Article
- DNA binding and transposition activity of the Sleeping Beauty transposase: role of structural stability of the primary DNA-binding domain.Nucleic acids research · 2025Article
- A novel hyperactive variant of theMolecular therapy. Nucleic acids · 2024Article
- Bioinformatic Annotation of Transposon DNA Processing Genes on the Long-Read Genome Assembly ofBioinformatics and biology insights · 2024Article
- Zinc-finger BED domains drive the formation of the active Hermes transpososome by asymmetric DNA binding.Nature communications · 2023Article
- IS21 family transposase cleaved donor complex traps two right-handed superhelical crossings.Nature communications · 2023Article
- Engineered Sleeping Beauty transposase redirects transposon integration away from genes.Nucleic acids research · 2022Article
- Structure and function of retroviral integrase.Nature reviews. Microbiology · 2022Review
- Structure, Activity, and Function of SETMAR Protein Lysine Methyltransferase.Life (Basel, Switzerland) · 2021Review
- The large bat Helitron DNA transposase forms a compact monomeric assembly that buries and protects its covalently bound 5'-transposon end.Molecular cell · 2021Article
- Recurrent evolution of vertebrate transcription factors by transposase capture.Science (New York, N.Y.) · 2021Article
- Jumping Ahead withViruses · 2021Review
- Structures of ISCth4 transpososomes reveal the role of asymmetry in copy-out/paste-in DNA transposition.The EMBO journal · 2021Article
- Retroviral integrase: Structure, mechanism, and inhibition.The Enzymes · 2021Article
- Structural basis for the activation and suppression of transposition during evolution of the RAG recombinase.The EMBO journal · 2020Article
37 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
A key step in cut-and-paste DNA transposition is the pairing of transposon ends before the element is excised and inserted at a new site in its host genome. Crystallographic analyses of the paired-end complex (PEC) formed from precleaved transposon ends and the transposase of the eukaryotic element Mos1 reveals two parallel ends bound to a dimeric enzyme. The complex has a trans arrangement, with each transposon end recognized by the DNA binding region of one transposase monomer and by the active site of the other monomer. Two additional DNA duplexes in the crystal indicate likely binding sites for flanking DNA. Biochemical data provide support for a model of the target capture complex and identify Arg186 to be critical for target binding. Mixing experiments indicate that a transposase dimer initiates first-strand cleavage and suggest a pathway for PEC formation.
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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.