Evidence map›Paper›PMID 28445788›Full record

ReviewCurrent opinion in cell biology2017

An emerging role for the ribosome as a nexus for post-translational modifications.

Deniz Simsek, Maria Barna

Abstract readReview
In one paragraph

Review in Current opinion in cell biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
86citing papers in PubMed, 1 pooled it
5.8field-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

86 citing papers in PubMed, 1 synthesis or guideline pooled it, 128 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Mapping the architecture of protein complexes inProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  4. RiboScreenBiomedicines · 2026
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Ribosome Molecular Aging Shapes Translation Dynamics.bioRxiv : the preprint server for biology · 2026
    Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. 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
  16. High-throughput approaches for the identification of ribosome heterogeneity.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025
    Review
  17. Impacts of ribosomal RNA sequence variation on gene expression and phenotype.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025
    Review
  18. Built differently or defective: can RNA exosomopathies cause ribosome heterogeneity?Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025
    Review
  19. Article
  20. Review

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

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.

Deniz SimsekDepartment of Developmental Biology, Stanford University, Stanford, CA 94305, USA; Department of Genetics, Stanford University, Stanford, CA 94305, USA.
Maria BarnaDepartment of Developmental Biology, Stanford University, Stanford, CA 94305, USA; Department of Genetics, Stanford University, Stanford, CA 94305, USA. Electronic address: mbarna@stanford.edu.
Stanford University · US

Funding

Specialized Translational Control of Stem Cell Differentiation and Embryonic DevelopmentR01HD086634 · NICHD · STANFORD UNIVERSITY · PI BARNA, MARIA · 2016 to 2025
$5.5M
Characterizing the ribosome code controlling gene expression and cell fate specificationR21HD086730 · NICHD · STANFORD UNIVERSITY · PI BARNA, MARIA · 2016 to 2017
$431k
NICHD NIH HHS R01 HD086634NICHD NIH HHS R21 HD086730
6 · The paper itself

Abstract

The ribosome is one of life's most ancient molecular machines that has historically been viewed as a backstage participant in gene regulation, translating the genetic code across all kingdoms of life in a rote-like fashion. However, recent studies suggest that intrinsic components of the ribosome can be regulated and diversified as a means to intricately control the expression of the cellular proteome. In this review, we discuss advances in the characterization of ribosome post-translational modifications (PTMs) from past to present. We specifically focus on emerging examples of ribosome phosphorylation and ubiquitylation, which are beginning to showcase that PTMs of the ribosome are versatile, may have functional consequences for translational control, and are intimately linked to human disease. We further highlight the key questions that remain to be addressed to gain a more complete picture of the array of ribosome PTMs and the upstream enzymes that control them, which may endow ribosomes with greater regulatory potential in gene regulation and control of cellular homeostasis.

Indexed as

PhosphorylationProtein Processing, Post-TranslationalUbiquitinationAnimalsGene Expression RegulationHumansMammalsProteomeRibosomesUbiquitinProteomeUbiquitin

Identifiers

PMID28445788
PMCPMC5731828
OpenAlexW2605873159

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.