Evidence map›Paper›PMID 38071940›Full record

ReviewCurrent opinion in structural biology2024

How the ribosome shapes cotranslational protein folding.

Ekaterina Samatova, Anton A Komar, Marina V Rodnina

Open access · hybridAbstract readReview
In one paragraph

Review in Current opinion in structural biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
5.7field-weighted citation impact, top 3% of its field
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

19 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Article
  3. RiboScreenBiomedicines · 2026
    Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. High-resolution reconstruction of aRNA (New York, N.Y.) · 2024
    Article
  16. 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
  17. Translation Rates and Protein Folding.Journal of molecular biology · 2024
    Review
  18. Article
  19. 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

3 authors at 3 institutions in 2 countries.

Ekaterina SamatovaDepartment of Physical Biochemistry, Max Planck Institute for Multidisciplinary Sciences, Goettingen 37077, Germany.
Anton A KomarCenter for Gene Regulation in Health and Disease, Department of Biological, Geological and Environmental Sciences, Cleveland State University, 2121 Euclid Avenue, Cleveland, OH 44115, USA; Department of Biochemistry and Center for RNA Science and Therapeutics, School of Medicine, Case Western Reserve University, Cleveland, OH 44106, USA.
Marina V RodninaDepartment of Physical Biochemistry, Max Planck Institute for Multidisciplinary Sciences, Goettingen 37077, Germany. Electronic address: rodnina@mpinat.mpg.de.
Cleveland State University · USMax Planck Institute for Multidisciplinary SciencesMax Planck Institute for the Study of Religious and Ethnic Diversity · DE

Funding

Safer and more effective FIX therapeutics: impact of codon optimizationR01HL151392 · NHLBI · CLEVELAND STATE UNIVERSITY · PI KOMAR, ANTON A. · 2020 to 2023
$1.5M
eIF2A in translational controlR01GM128981 · NIGMS · CLEVELAND STATE UNIVERSITY · PI KOMAR, ANTON A. · 2020 to 2023
$1.2M
NHLBI NIH HHS R01 HL151392NIGMS NIH HHS R01 GM128981
6 · The paper itself

Abstract

During protein synthesis, the growing nascent peptide chain moves inside the polypeptide exit tunnel of the ribosome from the peptidyl transferase center towards the exit port where it emerges into the cytoplasm. The ribosome defines the unique energy landscape of the pioneering round of protein folding. The spatial confinement and the interactions of the nascent peptide with the tunnel walls facilitate formation of secondary structures, such as α-helices. The vectorial nature of protein folding inside the tunnel favors local intra- and inter-molecular interactions, thereby inducing cotranslational folding intermediates that do not form upon protein refolding in solution. Tertiary structures start to fold in the lower part of the tunnel, where interactions with the ribosome destabilize native protein folds. The present review summarizes the recent progress in understanding the driving forces of nascent protein folding inside the tunnel and at the surface of the ribosome.

Indexed as

Protein FoldingRibosomesPeptidesProtein BiosynthesisProteinsPeptidesProteins

Identifiers

PMID38071940
PMCPMC12257957
OpenAlexW4389512726

What OpenQuestion holds

Textmetadata
LicenceTDM
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.