ArticleeLife2016
Coupling between the DEAD-box RNA helicases Ded1p and eIF4A.
Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
What it found
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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.
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.
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Who cites it
46 citing papers in PubMed, 74 citations in OpenAlex.
- Suppression of upstream ORF translation is not a widespread mechanism of translational stimulation by yeast helicase Ded1.Nucleic acids research · 2026Article
- Suppression of upstream ORF translation is not a widespread mechanism of translational stimulation by yeast helicase Ded1.bioRxiv : the preprint server for biology · 2026Article
- A genetic interaction between DED1 and HAT1 in Saccharomyces cerevisiae reveals a role for Hat1p in cytoplasmic RNA granule accumulation.G3 (Bethesda, Md.) · 2026Article
- Eukaryotic translation initiation factor 4F: functional properties and physiological role.Nucleic acids research · 2025Review
- Rapid remodeling of NTP levels enables immediate translational adaptation to energy stress in yeast.Molecular cell · 2025Article
- 40S ribosomal subunits scan mRNA for the start codon by one-dimensional diffusion.RNA (New York, N.Y.) · 2025Article
- DDX6 interacts with DDX3X to repress translation in microRNA-mediated silencing.Nucleic acids research · 2025Article
- High-resolution fleezers reveal duplex opening and stepwise assembly by an oligomer of the DEAD-box helicase Ded1p.Nature communications · 2025Article
- Analyses of translation factors Dbp1 and Ded1 reveal the cellular response to heat stress to be separable from stress granule formation.Cell reports · 2024Article
- A novel reporter for helicase activity in translation uncovers DDX3X interactions.RNA (New York, N.Y.) · 2024Article
- The Role of the RNA Helicase DDX3X in Medulloblastoma Progression.Biomolecules · 2024Review
- Article
- The molecular basis of translation initiation and its regulation in eukaryotes.Nature reviews. Molecular cell biology · 2024Review
- Repression ofbioRxiv : the preprint server for biology · 2024Article
- Cellular functions of eukaryotic RNA helicases and their links to human diseases.Nature reviews. Molecular cell biology · 2023Review
- The RGG motif proteins: Interactions, functions, and regulations.Wiley interdisciplinary reviews. RNA · 2023Review
- Rapid 40S scanning and its regulation by mRNA structure during eukaryotic translation initiation.Cell · 2022Article
- mRNA- and factor-driven dynamic variability controls eIF4F-cap recognition for translation initiation.Nucleic acids research · 2022Article
- Measuring the impact of cofactors on RNA helicase activities.Methods (San Diego, Calif.) · 2022Article
- The RNA Helicase Ded1 Regulates Translation and Granule Formation during Multiple Phases of Cellular Stress Responses.Molecular and cellular biology · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Eukaryotic translation initiation involves two conserved DEAD-box RNA helicases, eIF4A and Ded1p. Here we show that S. cerevisiae eIF4A and Ded1p directly interact with each other and simultaneously with the scaffolding protein eIF4G. We delineate a comprehensive thermodynamic framework for the interactions between Ded1p, eIF4A, eIF4G, RNA and ATP, which indicates that eIF4A, with and without eIF4G, acts as a modulator for activity and substrate preferences of Ded1p, which is the RNA remodeling unit in all complexes. Our results reveal and characterize an unexpected interdependence between the two RNA helicases and eIF4G, and suggest that Ded1p is an integral part of eIF4F, the complex comprising eIF4G, eIF4A, and eIF4E.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.