Evidence map›Paper›PMID 29731232›Full record

ArticleStructure (London, England : 1993)2018

Conformational Control of Translation Termination on the 70S Ribosome.

Egor Svidritskiy, Andrei A Korostelev

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2018. 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
2.1field-weighted citation impact, top 12% 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, 33 citations in OpenAlex.

  1. Article
  2. Article
  3. Mechanistic insights intobioRxiv : the preprint server for biology · 2026
    Article
  4. A cascade of structural rearrangements positions peptide release factor 2 for polypeptide hydrolysis on the ribosome.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. Article
  6. The Structural Dynamics of Translation.Annual review of biochemistry · 2022
    Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Ribosome Rescue Pathways in Bacteria.Frontiers in microbiology · 2021
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Mechanism of premature translation termination on a sense codon.The Journal of biological chemistry · 2018
    Article
  19. 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

2 authors at 1 institution in 1 country.

Egor SvidritskiyRNA Therapeutics Institute, University of Massachusetts Medical School, 368 Plantation St., Worcester, MA 01605, USA.
Andrei A KorostelevRNA Therapeutics Institute, University of Massachusetts Medical School, 368 Plantation St., Worcester, MA 01605, USA. Electronic address: andrei.korostelev@umassmed.edu.
University of Massachusetts Chan Medical School · US

Funding

Vector CoreP30DK047757 · NIDDK · UNIVERSITY OF PENNSYLVANIA · PI WILSON, JAMES M · 1993 to 2017
$18.0M
Structural bases for cellular stress responses mediated by stalled translationR01GM106105 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI KOROSTELEV, ANDREI · 2013 to 2017
$1.6M
Molecular principles of translation terminationR01GM107465 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI KOROSTELEV, ANDREI · 2015 to 2018
$1.3M
NIDDK NIH HHS P30 DK047757NIGMS NIH HHS R01 GM106105NIGMS NIH HHS R01 GM107465
6 · The paper itself

Abstract

Translation termination ensures proper lengths of cellular proteins. During termination, release factor (RF) recognizes a stop codon and catalyzes peptide release. Conformational changes in RF are thought to underlie accurate translation termination. However, structural studies of ribosome termination complexes have only captured RFs in a conformation that is consistent with the catalytically active state. Here, we employ a hyper-accurate RF1 variant to obtain crystal structures of 70S termination complexes that suggest a structural pathway for RF1 activation. We trapped RF1 conformations with the catalytic domain outside of the peptidyl-transferase center, while the codon-recognition domain binds the stop codon. Stop-codon recognition induces 30S decoding-center rearrangements that precede accommodation of the catalytic domain. The separation of codon recognition from the opening of the catalytic domain suggests how rearrangements in RF1 and in the ribosomal decoding center coordinate stop-codon recognition with peptide release, ensuring accurate translation termination.

Indexed as

Binding SitesCatalytic DomainCodon, TerminatorModels, MolecularPeptide Chain Termination, TranslationalPeptide Termination FactorsProtein BindingProtein ConformationRibosomesRibosome Subunits, Large, BacterialRibosome Subunits, Small, BacterialCodon, TerminatorPeptide Termination Factorsblasticidin Sclass I release factorsstop-codon recognitiontermination accuracy

Identifiers

PMID29731232
PMCPMC5990466
OpenAlexW2774545689

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.