Evidence map›Paper›PMID 24581494›Full record

ArticleCell2014

Dom34 rescues ribosomes in 3' untranslated regions.

Nicholas R Guydosh, Rachel Green

Open access · bronzeAbstract read
In one paragraph

Article in Cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 246 papers.

0numbers the graph read from it
0cells of the map it votes in
246citing papers in PubMed
17.1field-weighted citation impact, top 1% 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

246 citing papers in PubMed, 401 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Ribosome-associated quality control and related mechanisms.Nature structural & molecular biology · 2026
    Review
  10. Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. TheGenome research · 2025
    Article
  18. Interpreting ribosome dynamics during mRNA translation.The Journal of biological chemistry · 2025
    Review
  19. Article
  20. Eukaryotic Microproteins.Annual review of biochemistry · 2025
    Review

186 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Nicholas R GuydoshHoward Hughes Medical Institute, Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
Rachel GreenHoward Hughes Medical Institute, Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA. Electronic address: ragreen@jhmi.edu.
Howard Hughes Medical Institute · US

Funding

Molecular mechanism of the ribosome and functions of translational regulationZIADK075132 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI GUYDOSH, NICHOLAS · 2016 to 2025
$14.3M
Molecular mechanisms of ribosome pausing and the cellular responseR37GM059425 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI GREEN, RACHEL · 2014 to 2023
$3.5M
The role played by the RNAs and tRNAs in translationR01GM059425 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI GREEN, RACHEL · 1999 to 2013
$3.4M
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM059425NIGMS NIH HHS R37 GM059425
6 · The paper itself

Abstract

Ribosomes that stall before completing peptide synthesis must be recycled and returned to the cytoplasmic pool. The protein Dom34 and cofactors Hbs1 and Rli1 can dissociate stalled ribosomes in vitro, but the identity of targets in the cell is unknown. Here, we extend ribosome profiling methodology to reveal a high-resolution molecular characterization of Dom34 function in vivo. Dom34 removes stalled ribosomes from truncated mRNAs, but, in contrast, does not generally dissociate ribosomes on coding sequences known to trigger stalling, such as polyproline. We also show that Dom34 targets arrested ribosomes near the ends of 3' UTRs. These ribosomes appear to gain access to the 3' UTR via a mechanism that does not require decoding of the mRNA. These results suggest that ribosomes frequently enter downstream noncoding regions and that Dom34 carries out the important task of rescuing them.

Indexed as

3' Untranslated RegionsCell Cycle ProteinsDiamideEndoribonucleasesNuclease Protection AssaysProtein BiosynthesisRibosomesSaccharomyces cerevisiaeSaccharomyces cerevisiae Proteins3' Untranslated RegionsCell Cycle ProteinsDiamideDom34 protein, S cerevisiaeEndoribonucleasesSaccharomyces cerevisiae Proteins

Identifiers

PMID24581494
PMCPMC4022138
OpenAlexW2020663470

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.