Evidence map›Paper›PMID 9144215›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1997

The p20 and Ded1 proteins have antagonistic roles in eIF4E-dependent translation in Saccharomyces cerevisiae.

J de la Cruz, I Iost, D Kressler, P Linder

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 115 papers.

0numbers the graph read from it
0cells of the map it votes in
115citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

115 citing papers in PubMed, 211 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Mistranslating tRNA variants impact the proteome and phosphoproteome ofbioRxiv : the preprint server for biology · 2025
    Article
  5. Article
  6. Article
  7. Repression ofbioRxiv : the preprint server for biology · 2024
    Article
  8. Article
  9. Surveying the global landscape of post-transcriptional regulators.Nature structural & molecular biology · 2023
    Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. eIF4E and Interactors from Unicellular Eukaryotes.International journal of molecular sciences · 2020
    Review
  19. Article
  20. Article

55 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

4 authors.

J de la CruzDépartement de Biochimie Médicale, CMU, 1, rue Michel Servet, 1211 Genève 4, Switzerland.
I Iost
D Kressler
P Linder

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The translation initiation factor eIF4E mediates the binding of the small ribosomal subunit to the cap structure at the 5' end of the mRNA. In Saccharomyces cerevisiae, the cap-binding protein eIF4E is mainly associated with eIF4G, forming the cap-binding complex eIF4F. Other proteins are detected upon purification of the complex on cap-affinity columns. Among them is p20, a protein of unknown function encoded by the CAF20 gene. Here, we show a negative regulatory role for the p20 protein in translation initiation. Deletion of CAF20 partially suppresses mutations in translation initiation factors. Overexpression of the p20 protein results in a synthetic enhancement of translation mutation phenotypes. Similar effects are observed for mutations in the DED1 gene, which we have isolated as a multicopy suppressor of a temperature-sensitive eIF4E mutation. The DED1 gene encodes a putative RNA helicase of the DEAD-box family. The analyses of its suppressor activity, of polysome profiles of ded1 mutant strains, and of synthetic lethal interactions with different translation mutants indicate that the Ded1 protein has a role in translation initiation in S. cerevisiae.

Indexed as

Gene Expression Regulation, FungalGenes, SuppressorProtein BiosynthesisCloning, MolecularDNA PrimersEscherichia coliEukaryotic Initiation Factor-4EGenes, FungalGenes, LethalMutagenesisPeptide Initiation FactorsPolymerase Chain ReactionPolyribosomesRNA-Binding ProteinsRNA Cap-Binding ProteinsRNA HelicasesDNA PrimersEukaryotic Initiation Factor-4EPeptide Initiation FactorsRNA-Binding ProteinsRNA Cap-Binding ProteinsRNA HelicasesRNA Nucleotidyltransferases

Identifiers

PMID9144215
PMCPMC24656
OpenAlexW2150540364

What OpenQuestion holds

Textmetadata
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.