Evidence map›Paper›PMID 31819057›Full record

ArticleNature communications2019

Oxidation and alkylation stresses activate ribosome-quality control.

Liewei L Yan, Carrie L Simms, Fionn McLoughlin, Richard D Vierstra, Hani S Zaher

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers.

0numbers the graph read from it
0cells of the map it votes in
79citing papers in PubMed
3.6field-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

79 citing papers in PubMed, 120 citations in OpenAlex.

  1. Article
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  4. Article
  5. Review
  6. Article
  7. Quality control and signaling pathways at stalled ribosomes.Experimental & molecular medicine · 2026
    Review
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19 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

5 authors at 1 institution in 1 country.

Liewei L YanDepartment of Biology, Washington University in St. Louis, St. Louis, MO, 63130, USA.ORCID http://orcid.org/0000-0002-3692-0621
Carrie L SimmsDepartment of Biology, Washington University in St. Louis, St. Louis, MO, 63130, USA.
Fionn McLoughlinDepartment of Biology, Washington University in St. Louis, St. Louis, MO, 63130, USA.ORCID http://orcid.org/0000-0002-2430-5074
Richard D VierstraDepartment of Biology, Washington University in St. Louis, St. Louis, MO, 63130, USA.
Hani S ZaherDepartment of Biology, Washington University in St. Louis, St. Louis, MO, 63130, USA. hzaher@wustl.edu.
Washington University in St. Louis · US

Funding

THE ROLE OF THE RIBOSOME IN DETERMINING THE FATE OF DAMAGED MRNA-SupplementR01GM112641 · NIGMS · WASHINGTON UNIVERSITY · PI ZAHER, HANI · 2015 to 2024
$3.1M
6 · The paper itself

Abstract

Oxidation and alkylation of nucleobases are known to disrupt their base-pairing properties within RNA. It is, however, unclear whether organisms have evolved general mechanism(s) to deal with this damage. Here we show that the mRNA-surveillance pathway of no-go decay and the associated ribosome-quality control are activated in response to nucleobase alkylation and oxidation. Our findings reveal that these processes are important for clearing chemically modified mRNA and the resulting aberrant-protein products. In the absence of Xrn1, the level of damaged mRNA significantly increases. Furthermore, deletion of LTN1 results in the accumulation of protein aggregates in the presence of oxidizing and alkylating agents. This accumulation is accompanied by Hel2-dependent regulatory ubiquitylation of ribosomal proteins. Collectively, our data highlight the burden of chemically damaged mRNA on cellular homeostasis and suggest that organisms evolved mechanisms to counter their accumulation.

Indexed as

Oxidative Stress4-Nitroquinoline-1-oxideAlkylationDNA AdductsDNA DamageHEK293 CellsHumansMethyl MethanesulfonateMutationOxidation-ReductionPeptidesPolyribosomesProtein AggregatesQuinolonesRibosomal ProteinsRibosomes4-Nitroquinoline-1-oxide4-nitroquinolone-1-oxideDNA AdductsHel2 protein, S cerevisiaeMethyl MethanesulfonatePeptidesProtein AggregatesQuinolonesRibosomal ProteinsRNA, MessengerSaccharomyces cerevisiae ProteinsUbiquitinUbiquitin-Protein Ligases

Identifiers

PMID31819057
PMCPMC6901537
OpenAlexW2993298108

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.