ArticleCell2019
Cryo-EM Structures of a Group II Intron Reverse Splicing into DNA.
Article in Cell, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
45 citing papers in PubMed, 71 citations in OpenAlex.
- Self-splicing and cyclization mechanisms of the full-length Anabaena pre-tRNA.Nature chemical biology · 2026Article
- Recurrent Modular Assembly Drives Independent Origins of Group II Introns Encoding LAGLIDADG Homing Endonucleases.Genome biology and evolution · 2026Article
- Structural Remodeling and Enzymatic Replacement Shape the Evolution of Organellar Group II Introns inInternational journal of molecular sciences · 2026Article
- RNA Triple Helices: From Structures and Mechanisms to Therapeutic Targets.International journal of biological sciences · 2026Review
- Pre-mRNA splicing and its regulation in microalgae and cyanobacteria.Advanced biotechnology · 2025Review
- Article
- Cysteine Mutagenesis of a Group II Intron-Encoded Protein Supports Splicing, Mobility, and Site-Specific Labeling.Biochemistry · 2025Article
- Structural basis for the evolution of a domesticated group II intron-like reverse transcriptase to function in host cell DNA repair.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- ARTEM: a method for RNA and DNA tertiary motif identification with backbone permutations.Genome biology · 2025Article
- Computational De Novo Design of Group II Introns Yields Highly Active Ribozymes.Chembiochem : a European journal of chemical biology · 2025Article
- Structures of vertebrate R2 retrotransposon complexes during target-primed reverse transcription and after second-strand nicking.Science advances · 2025Article
- Structural and biochemical studies of mobile retrotransposon proteins in action.Current opinion in structural biology · 2025Review
- Structures of a natural circularly permuted group II intron reveal mechanisms of branching and backsplicing.Nature structural & molecular biology · 2025Article
- Structural basis of circularly permuted group II intron self-splicing.Nature structural & molecular biology · 2025Article
- Ensemble refinement of mismodeled cryo-EM RNA structures using all-atom simulations.Nature communications · 2025Article
- Article
- Scaffold-enabled high-resolution cryo-EM structure determination of RNA.Nature communications · 2025Article
- Protein-free catalysis of DNA hydrolysis and self-integration by a ribozyme.Nucleic acids research · 2025Article
- Review
- Targeting the conserved active site of splicing machines with specific and selective small molecule modulators.Nature communications · 2024Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Group II introns are a class of retroelements that invade DNA through a copy-and-paste mechanism known as retrotransposition. Their coordinated activities occur within a complex that includes a maturase protein, which promotes splicing through an unknown mechanism. The mechanism of splice site exchange within the RNA active site during catalysis also remains unclear. We determined two cryo-EM structures at 3.6-Å resolution of a group II intron reverse splicing into DNA. These structures reveal that the branch-site domain VI helix swings 90°, enabling substrate exchange during DNA integration. The maturase assists catalysis through a transient RNA-protein contact with domain VI that positions the branch-site adenosine for lariat formation during forward splicing. These findings provide the first direct evidence of the role the maturase plays during group II intron catalysis. The domain VI dynamics closely parallel spliceosomal branch-site helix movement and provide strong evidence for a retroelement origin of the spliceosome.
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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.