Evidence map›Paper›PMID 22855532›Full record

ArticleMolecular biology of the cell2012

The essential iron-sulfur protein Rli1 is an important target accounting for inhibition of cell growth by reactive oxygen species.

Alawiah Alhebshi, Theodora C Sideri, Sara L Holland, Simon V Avery

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

42 citing papers in PubMed, 72 citations in OpenAlex.

  1. Article
  2. The function of Mak16 in ribosome biogenesis depends on its [4Fe-4S] cluster.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Review
  4. Article
  5. Article
  6. Rebirth of the translational machinery: The importance of recycling ribosomes.BioEssays : news and reviews in molecular, cellular and developmental biology · 2022
    Article
  7. Review
  8. Review
  9. Article
  10. Impact of Hydrogen Peroxide on Protein Synthesis in Yeast.Antioxidants (Basel, Switzerland) · 2021
    Review
  11. Review
  12. Article
  13. New Insights inToxins · 2020
    Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. 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

4 authors at 1 institution in 1 country.

Alawiah AlhebshiSchool of Biology, University of Nottingham, Nottingham, United Kingdom.
Theodora C Sideri
Sara L Holland
Simon V Avery
University of Nottingham · GB

Funding

Role of Oxidative Mechanisms in the Toxicity of MetalsR01GM057945 · NIGMS · UNIVERSITY OF NOTTINGHAM · PI AVERY, SIMON V · 1999 to 2007
$1.4M
Biotechnology and Biological Sciences Research Council BB/I000852/1NIGMS NIH HHS R01 GM057945NIGMS NIH HHS R01 GM57945
6 · The paper itself

Abstract

Oxidative stress mediated by reactive oxygen species (ROS) is linked to degenerative conditions in humans and damage to an array of cellular components. However, it is unclear which molecular target(s) may be the primary "Achilles' heel" of organisms, accounting for the inhibitory action of ROS. Rli1p (ABCE1) is an essential and highly conserved protein of eukaryotes and archaea that requires notoriously ROS-labile cofactors (Fe-S clusters) for its functions in protein synthesis. In this study, we tested the hypothesis that ROS toxicity is caused by Rli1p dysfunction. In addition to being essential, Rli1p activity (in nuclear ribosomal-subunit export) was shown to be impaired by mild oxidative stress in yeast. Furthermore, prooxidant resistance was decreased by RLI1 repression and increased by RLI1 overexpression. This Rlip1 dependency was abolished during anaerobicity and accentuated in cells expressing a FeS cluster-defective Rli1p construct. The protein's FeS clusters appeared ROS labile during in vitro incubations, but less so in vivo. Instead, it was primarily (55)FeS-cluster supply to Rli1p that was defective in prooxidant-exposed cells. The data indicate that, owing to its essential nature but dependency on ROS-labile FeS clusters, Rli1p function is a primary target of ROS action. Such insight could help inform new approaches for combating oxidative stress-related disease.

Indexed as

ATP-Binding Cassette TransportersBlotting, WesternCell DivisionCopperCycloheximideGene Expression Regulation, DevelopmentalGene Expression Regulation, FungalGenes, EssentialGreen Fluorescent ProteinsIron-Sulfur ProteinsMicroscopy, FluorescenceMutationProtein TransportReactive Oxygen SpeciesReverse Transcriptase Polymerase Chain ReactionRibosomal ProteinsATP-Binding Cassette TransportersCopperCycloheximideGreen Fluorescent ProteinsIron-Sulfur ProteinsReactive Oxygen SpeciesRibosomal ProteinsRLI1 protein, S cerevisiaeRps2 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID22855532
PMCPMC3442406
OpenAlexW2086807456

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.