ArticleThe Journal of biological chemistry2020
The folding and unfolding behavior of ribonuclease H on the ribosome.
Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 33 citations in OpenAlex.
- 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
- Cotranslational protein folding through non-native structural intermediates.Science advances · 2025Article
- Arrest Peptide Profiling resolves co-translational folding pathways and chaperone interactions in vivo.Nature communications · 2025Article
- Beyond Misfolding: A New Paradigm for the Relationship Between Protein Folding and Aggregation.International journal of molecular sciences · 2024Review
- Resolving chaperone-assisted protein folding on the ribosome at the peptide level.Nature structural & molecular biology · 2024Article
- Article
- Translation Rates and Protein Folding.Journal of molecular biology · 2024Review
- AutoRNC: An automated modeling program for building atomic models of ribosome-nascent chain complexes.Structure (London, England : 1993) · 2024Article
- The SecM arrest peptide traps a pre-peptide bond formation state of the ribosome.Nature communications · 2024Article
- How the ribosome shapes cotranslational protein folding.Current opinion in structural biology · 2024Review
- Cell-Free Synthesis Strategies to Probe Co-translational Folding of Proteins Within Lipid Membranes.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Interactions between nascent proteins and the ribosome surface inhibit co-translational folding.Nature chemistry · 2021Article
- The driving force for co-translational protein folding is weaker in the ribosome vestibule due to greater water ordering.Chemical science · 2021Article
- Co-translational folding of nascent polypeptides: Multi-layered mechanisms for the efficient biogenesis of functional proteins.BioEssays : news and reviews in molecular, cellular and developmental biology · 2021Article
- Fundamentals to function: Quantitative and scalable approaches for measuring protein stability.Cell systems · 2021Review
- Cotranslational folding of alkaline phosphatase in the periplasm of Escherichia coli.Protein science : a publication of the Protein Society · 2020Article
- A protein folding intermediate pulls its weight.The Journal of biological chemistry · 2020Article
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5 authors at 3 institutions in 2 countries.
Funding
Abstract
The health of a cell depends on accurate translation and proper protein folding, whereas misfolding can lead to aggregation and disease. The first opportunity for a protein to fold occurs during translation, when the ribosome and surrounding environment can affect the nascent chain energy landscape. However, quantifying these environmental effects is challenging because ribosomal proteins and rRNA preclude most spectroscopic measurements of protein energetics. Here, we have applied two gel-based approaches, pulse proteolysis and force-profile analysis, to probe the folding and unfolding pathways of RNase H (RNH) nascent chains stalled on the prokaryotic ribosome
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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.