ArticleNature structural & molecular biology2026
Structures of protein folding intermediates on the ribosome.
Article in Nature structural & molecular biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Quasi-continuous cotranslational compaction and folding of a multidomain protein.Nature communications · 2026Article
- A detailed molecular picture of protein folding during active translation.bioRxiv : the preprint server for biology · 2026Article
- Evolution of the ribosomal exit tunnel through the eyes of the nascent chain.Nucleic acids research · 2026Article
- Structures of protein folding intermediates on the ribosome.Nature structural & molecular biology · 2026Article
- Rational design ofNature communications · 2025Article
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9 authors.
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Abstract
The ribosome biases the conformations sampled by nascent polypeptide chains along folding pathways toward biologically active states. A hallmark of the cotranslational folding (coTF) of many proteins constitutes highly stable folding intermediates that are absent or only transiently populated off the ribosome, yet persist during translation well beyond complete emergence of the domain from the ribosome exit tunnel. Despite the importance of intermediates for folding fidelity, their structures have remained elusive and cannot be predicted by machine learning methods. Here we obtained structures of two folding intermediates of an immunoglobulin-like domain on the ribosome by developing comprehensive
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