Evidence map›Paper›PMID 32050486›Full record

ReviewInternational journal of molecular sciences2020

Expanding Role of Ubiquitin in Translational Control.

Shannon E Dougherty, Austin O Maduka, Toshifumi Inada, Gustavo M Silva

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
3.5field-weighted citation impact, top 6% 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

48 citing papers in PubMed, 70 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. The Role of the Ubiquitin System in Eye Diseases.Life (Basel, Switzerland) · 2025
    Review
  9. Ribosome-associated proteins: unwRAPping ribosome heterogeneity in the twenty-first century.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025
    Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Review
  18. Article
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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

4 authors at 2 institutions in 2 countries.

Shannon E DoughertyDepartment of Biology, Duke University, Durham, NC 27708-0338, USA.
Austin O MadukaDepartment of Biology, Duke University, Durham, NC 27708-0338, USA.ORCID 0000-0001-7714-8677
Toshifumi InadaGraduate School of Pharmaceutical Sciences, Tohoku University, Sendai 980-8578, Japan.
Gustavo M SilvaDepartment of Biology, Duke University, Durham, NC 27708-0338, USA.
Duke University · USTohoku University · JP

Funding

MEDICAL SCIENTIST TRAINING PROGRAMT32GM007171 · NIGMS · DUKE UNIVERSITY · PI KONTOS, CHRISTOPHER D · 1985 to 2021
$31.2M
Resource for Biocomputing Visualization and InformaticsP41GM103311 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FERRIN, THOMAS E · 2012 to 2017
$8.2M
Defining the roles of ubiquitination during the environmental stress responseR00ES025835 · NIEHS · DUKE UNIVERSITY · PI SILVA, GUSTAVO M · 2018 to 2020
$905k
Defining the roles of ubiquitination during the environmental stress responseK99ES025835 · NIEHS · NEW YORK UNIVERSITY · PI SILVA, GUSTAVO M · 2015 to 2016
$205k
NIEHS NIH HHS ES025835NIEHS NIH HHS R00 ES025835NIGMS NIH HHS P41 GM103311NIGMS NIH HHS T32 GM007171
6 · The paper itself

Abstract

The eukaryotic proteome has to be precisely regulated at multiple levels of gene expression, from transcription, translation, and degradation of RNA and protein to adjust to several cellular conditions. Particularly at the translational level, regulation is controlled by a variety of RNA binding proteins, translation and associated factors, numerous enzymes, and by post-translational modifications (PTM). Ubiquitination, a prominent PTM discovered as the signal for protein degradation, has newly emerged as a modulator of protein synthesis by controlling several processes in translation. Advances in proteomics and cryo-electron microscopy have identified ubiquitin modifications of several ribosomal proteins and provided numerous insights on how this modification affects ribosome structure and function. The variety of pathways and functions of translation controlled by ubiquitin are determined by the various enzymes involved in ubiquitin conjugation and removal, by the ubiquitin chain type used, by the target sites of ubiquitination, and by the physiologic signals triggering its accumulation. Current research is now elucidating multiple ubiquitin-mediated mechanisms of translational control, including ribosome biogenesis, ribosome degradation, ribosome-associated protein quality control (RQC), and redox control of translation by ubiquitin (RTU). This review discusses the central role of ubiquitin in modulating the dynamism of the cellular proteome and explores the molecular aspects responsible for the expanding puzzle of ubiquitin signals and functions in translation.

Indexed as

Protein BiosynthesisUbiquitinationAnimalsHumansModels, MolecularOxidative StressProteasome Endopeptidase ComplexProteolysisRibosomal ProteinsRibosomesRNA StabilityUbiquitinProteasome Endopeptidase ComplexRibosomal ProteinsUbiquitindegradationoxidative stressquality controlribosomal proteinribosometranslation regulationubiquitin

Identifiers

PMID32050486
PMCPMC7037965
OpenAlexW3005128549

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.