Evidence map›Paper›PMID 33953328›Full record

ArticleCommunications biology2021

The ribosome modulates folding inside the ribosomal exit tunnel.

Florian Wruck, Pengfei Tian, Renuka Kudva, Robert B Best, Gunnar von Heijne, Sander J Tans, Alexandros Katranidis

Abstract read
In one paragraph

Article in Communications biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

34 citing papers in PubMed.

  1. Article
  2. Article
  3. Structures of protein folding intermediates on the ribosome.Nature structural & molecular biology · 2026
    Article
  4. Review
  5. Article
  6. Article
  7. Trigger factor accelerates nascent chain compaction and folding.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Article
  9. Article
  10. Remodelled ribosomal populations synthesize a specific proteome in proliferating plant tissue during cold.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025
    Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. How the ribosome shapes cotranslational protein folding.Current opinion in structural biology · 2024
    Review
  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors.

Florian WruckAMOLF, Amsterdam, The Netherlands.
Pengfei TianProtein Engineering, Novozymes A/S, Lyngby, Denmark.
Renuka KudvaDepartment of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.ORCID 0000-0003-0426-3716
Robert B BestLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health (NIH), Bethesda, MD, USA.ORCID 0000-0002-7893-3543
Gunnar von HeijneDepartment of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.
Sander J TansAMOLF, Amsterdam, The Netherlands. tans@amolf.nl.
Alexandros KatranidisInstitute of Biological Information Processing IBI-6, Forschungszentrum Jülich (FZJ), Jülich, Germany. a.katranidis@fz-juelich.de.ORCID 0000-0002-1785-1659

Funding

Understanding protein folding, evolution and function via molecular simulationZIADK075104 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI BEST, ROBERT · 2013 to 2025
$13.7M
6 · The paper itself

Abstract

Proteins commonly fold co-translationally at the ribosome, while the nascent chain emerges from the ribosomal exit tunnel. Protein domains that are sufficiently small can even fold while still located inside the tunnel. However, the effect of the tunnel on the folding dynamics of these domains is not well understood. Here, we combine optical tweezers with single-molecule FRET and molecular dynamics simulations to investigate folding of the small zinc-finger domain ADR1a inside and at the vestibule of the ribosomal tunnel. The tunnel is found to accelerate folding and stabilize the folded state, reminiscent of the effects of chaperonins. However, a simple mechanism involving stabilization by confinement does not explain the results. Instead, it appears that electrostatic interactions between the protein and ribosome contribute to the observed folding acceleration and stabilization of ADR1a.

Indexed as

Molecular Dynamics SimulationProtein BiosynthesisProtein FoldingDNA-Binding ProteinsProtein DomainsRibosomesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscription FactorsADR1 protein, S cerevisiaeDNA-Binding ProteinsSaccharomyces cerevisiae ProteinsTranscription Factors

Identifiers

PMID33953328
PMCPMC8100117

What OpenQuestion holds

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Registered trials

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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.