ArticleNature communications2025
A rapid, simple, and economical method for the isolation of ribosomes and translational machinery for structural and functional studies.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- A human cell-free translation screen identifies the NT-2 mycotoxin as a ribosomal inhibitor that binds the peptidyl transferase center.Communications biology · 2026Article
- hY3 RNA binds and inhibits ribosomes and modulates the starvation-induced integrated stress response.Nucleic acids research · 2026Article
- Rapid plastid isolation reveals the chloroplast proteome and structures of the chlororibosome large subunit and RuBisCO inbioRxiv : the preprint server for biology · 2026Article
- A family of archaeal hibernation factors that bind in tandem and protect ribosomes in dormant cells.Nature communications · 2026Article
- RiboScreenBiomedicines · 2026Review
- Ribosome heterogeneity and specialization in musculoskeletal physiology and pathology.JBMR plus · 2026Article
- Article
- A family of archaeal hibernation factors that bind in tandem and protect ribosomes in dormant cells.bioRxiv : the preprint server for biology · 2026Article
- Purification of ribosomes from human embryonic stem (hES) cells for high-resolution Cryo-EM structural studies.Frontiers in molecular biosciences · 2026Article
- Evolution of ribosome X-ray crystallography: from first crystals to atomic resolution.Biophysical reviews · 2025Review
- Ribosome heterogeneity and specialization.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025Article
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11 authors.
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Abstract
Ribosomes are RNA-protein complexes essential for protein synthesis and quality control. Traditional methods for ribosome isolation are labor-intensive, expensive, and require a substantial amount of biological material. In contrast, our method, RNA affinity purification using poly-lysine (RAPPL), provides a rapid, simple, and cost-effective alternative applicable to various species and types of starting material (cell lysates, whole cells, organs, or whole organisms). It is also compatible with traditional isolation techniques. Here, we describe the use of RAPPL for rapid isolation, functional screening, and structural analysis of ribosomes and associated factors. We also demonstrate the application of RAPPL in investigating ribosome-associated resistance mechanisms in uropathogenic Escherichia coli samples and generating a 2.7-Å cryoEM ribosome structure from Cryptococcus neoformans. By significantly reducing the amount of the starting biological material and the time required for isolation, RAPPL has the potential to facilitate the study of ribosomal function, interactions, and antibiotic resistance and provide a versatile platform for academic, clinical, and industrial research.
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