ArticleJournal of molecular biology2018
Serine Integrase attP Binding and Specificity.
Article in Journal of molecular biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 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
20 citing papers in PubMed, 29 citations in OpenAlex.
- Retargeted serine integrases for one-step, precise integration of large DNA sequences in human cells.Nature biotechnology · 2026Article
- Modular gene tagging inResearch square · 2026Article
- Modular gene tagging inbioRxiv : the preprint server for biology · 2026Article
- Directed evolution on compact landing pads yields highly efficient recombinases for large DNA integration.Nucleic acids research · 2026Article
- Plasmid2MC: efficient cell-free generation of high-purity minicircle DNA for genome editing in mammalian cells.Communications biology · 2025Article
- Site-specific DNA insertion into the human genome with engineered recombinases.Nature biotechnology · 2025Article
- Structural basis of directionality control in large serine integrases.bioRxiv : the preprint server for biology · 2025Article
- Efficient site-specific integration of large genes in mammalian cells via continuously evolved recombinases and prime editing.Nature biomedical engineering · 2025Article
- There and turn back again: the application of phage serine integrases in eukaryotic systems.Frontiers in bioengineering and biotechnology · 2025Review
- Directed evolution of hyperactive integrases for site specific insertion of transgenes.Nucleic acids research · 2024Article
- Directed evolution of hyperactive integrases for site specific insertion of transgenes.bioRxiv : the preprint server for biology · 2024Article
- Engineering intelligent chassis cells via recombinase-based MEMORY circuits.Nature communications · 2024Article
- Article
- The influence of coiled-coil motif of serine recombinase toward the directionality regulation.Biophysical journal · 2023Article
- Next generation synthetic memory via intercepting recombinase function.Nature communications · 2023Article
- Model-guided engineering of DNA sequences with predictable site-specific recombination rates.Nature communications · 2022Article
- Efficient targeted transgenesis of large donor DNA into multiple mouse genetic backgrounds using bacteriophage Bxb1 integrase.Scientific reports · 2022Article
- Control of the Serine Integrase Reaction: Roles of the Coiled-Coil and Helix E Regions in DNA Site Synapsis and Recombination.Journal of bacteriology · 2021Article
- A bipartite thermodynamic-kinetic contribution by an activating mutation to RDF-independent excision by a phage serine integrase.Nucleic acids research · 2020Article
- High-resolution specificity profiling and off-target prediction for site-specific DNA recombinases.Nature communications · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Serine integrases catalyze the site-specific insertion of viral DNA into a host's genome. The minimal requirements and irreversible nature of this integration reaction have led to the use of serine integrases in applications ranging from bacterial memory storage devices to gene therapy. Our understanding of how the integrase proteins recognize the viral (attP) and host (attB) attachment sites is limited, with structural data available for only a Listeria integrase C-terminal domain (CTD) bound to an attP half-site. Here we report quantitative binding and saturation mutagenesis analyses for the Listeria innocua prophage attP site and a new 2.8-Å crystal structure of the CTD•attP half site. We find that Int binds with high affinity to attP (6.9 nM), but the Int CTD binds to attP half-sites with only 7- to 10-fold lower affinity, supporting the idea that free energy is expended to open an Int dimer for attP binding. Despite the 50-bp Int-attP interaction surface, only 20 residues are sensitive to mutagenesis, and of these, only 6 require a specific residue for efficient Int binding and integration activity. One of the integrase DNA-binding domains, the recombinase domain, appears to be primarily non-specific. Several substitutions result in an improved attP site, indicating that higher-efficiency attachment sites can be obtained through site engineering. These findings advance our understanding of serine integrase function and provide important data for efforts towards engineering this family of enzymes for a variety of biotechnology applications.
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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.