Evidence map›Paper›PMID 30475203›Full record

ArticleeLife2018

The shape of the bacterial ribosome exit tunnel affects cotranslational protein folding.

Renuka Kudva, Pengfei Tian, Fátima Pardo-Avila, Marta Carroni, Robert B Best, Harris D Bernstein, Gunnar von Heijne

Abstract read
In one paragraph

Article in eLife, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing 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

44 citing papers in PubMed.

  1. Article
  2. Structures of protein folding intermediates on the ribosome.Nature structural & molecular biology · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Exploring metalloproteome remodeling in calprotectin-stressedbioRxiv : the preprint server for biology · 2025
    Article
  7. Article
  8. Article
  9. Article
  10. The importance of the location of the N-terminus in successful protein folding in vivo and in vitro.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  11. Article
  12. Translation Rates and Protein Folding.Journal of molecular biology · 2024
    Review
  13. Force-regulated chaperone activity of BiP/ERdj3 is opposite to their homologs DnaK/DnaJ.Protein science : a publication of the Protein Society · 2024
    Article
  14. Article
  15. How the ribosome shapes cotranslational protein folding.Current opinion in structural biology · 2024
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
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.

Renuka KudvaDepartment of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.ORCID http://orcid.org/0000-0003-0426-3716
Pengfei TianLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, United States.
Fátima Pardo-AvilaDepartment of Structural Biology, Stanford University, Stanford, United States.
Marta CarroniDepartment of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.ORCID http://orcid.org/0000-0002-7697-6427
Robert B BestLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, United States.ORCID https://orcid.org/0000-0002-7893-3543
Harris D BernsteinGenetics and Biochemistry Branch, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, United States.ORCID http://orcid.org/0000-0002-4941-3741
Gunnar von HeijneDepartment of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.ORCID http://orcid.org/0000-0002-4490-8569

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
Emergent Properties of Complex Systems: From Atoms to Macromolecules; from Humans to SocietiesR35GM122543 · NIGMS · STANFORD UNIVERSITY · PI MICHAEL LEVITT · 2017 to 2026
$5.1M
NIGMS NIH HHS R35 GM122543NIH HHS IntramuralNIH HHS R35GM122543
6 · The paper itself

Abstract

The

Indexed as

Protein FoldingEscherichia coliMolecular Dynamics SimulationProtein BiosynthesisProtein DomainsRibosomesZinc Fingersarrest peptidebiochemistrychemical biologycotranslationalE. colimolecular biophysicsprotein foldingribosomestructural biologyuL23uL24

Identifiers

PMID30475203
PMCPMC6298777

What OpenQuestion holds

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Read underepoch 390

Registered trials

None linked

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.