ReviewRNA biology2013
The DEAD-box helicase eIF4A: paradigm or the odd one out?
Review in RNA biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers, 1 of them a synthesis that pooled it.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
84 citing papers in PubMed, 1 synthesis or guideline pooled it, 129 citations in OpenAlex.
- Pooled it
- Rocaglates and pateamines target the DEAD-box RNA helicase eIF4A from Schistosoma mansoni and demonstrate anti-schistosomal activity in vitro.Scientific reports · 2026Article
- Remodeling of mRNA by eIF4F in human translation initiation.bioRxiv : the preprint server for biology · 2026Article
- Nanometer-scale RNA protein clusters (RPCs) Foster Helicase Activity of DEAD-box eIF4A.bioRxiv : the preprint server for biology · 2026Article
- Targeted Intracellular Delivery of Amino Acids to Trophoblast Cells Reveals Proteomic Signatures of Cellular Utilisation.Biomolecules · 2026Article
- Eukaryotic translation initiation factor 4F: functional properties and physiological role.Nucleic acids research · 2025Review
- BLF1 Affects ATP Hydrolysis Catalyzed by Native and Mutated eIF4A1 and eIF4A2 Proteins.Toxins · 2025Article
- Characterization and Early Response of the DEAD Gene Family to Heat Stress in Tomato.Plants (Basel, Switzerland) · 2025Article
- Circadian Control of Protein Synthesis.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025Review
- The ATPase activity of yeast chromosome axis protein Hop1 affects the frequency of meiotic crossovers.Nucleic acids research · 2025Article
- The DEAD-box RNA helicase eIF4A is a crucial factor for stem-cell activity and reproduction of the parasiteFrontiers in cellular and infection microbiology · 2025Article
- Article
- Analyses of translation factors Dbp1 and Ded1 reveal the cellular response to heat stress to be separable from stress granule formation.Cell reports · 2024Article
- eIF4E orchestrates mRNA processing, RNA export and translation to modify specific protein production.Nucleus (Austin, Tex.) · 2024Review
- Protein-RNA interactions mediated by silvestrol-insight into a unique molecular clamp.Nucleic acids research · 2024Article
- Radiation-sensitive circRNA hsa_circ_0096498 inhibits radiation-induced liver fibrosis by suppressing EIF4A3 nuclear translocation to decrease CDC42 expression in hepatic stellate cells.Journal of translational medicine · 2024Article
- eIF4A1 enhances LARP1-mediated translational repression during mTORC1 inhibition.Nature structural & molecular biology · 2024Article
- DEAD-box RNA helicases in the multistep process of tumor metastasis.Molecular biology reports · 2024Review
- PABP-driven secondary condensed phase within RSV inclusion bodies activates viral mRNAs for ribosomal recruitment.Virologica Sinica · 2024Article
- The molecular basis of translation initiation and its regulation in eukaryotes.Nature reviews. Molecular cell biology · 2024Review
24 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
DEAD-box helicases catalyze the ATP-dependent unwinding of RNA duplexes. They share a helicase core formed by two RecA-like domains that carries a set of conserved motifs contributing to ATP binding and hydrolysis, RNA binding and duplex unwinding. The translation initiation factor eIF4A is the founding member of the DEAD-box protein family, and one of the few examples of DEAD-box proteins that consist of a helicase core only. It is an RNA-stimulated ATPase and a non-processive helicase that unwinds short RNA duplexes. In the catalytic cycle, a series of conformational changes couples the nucleotide cycle to RNA unwinding. eIF4A has been considered a paradigm for DEAD-box proteins, and studies of its function have revealed the governing principles underlying the DEAD-box helicase mechanism. However, as an isolated helicase core, eIF4A is rather the exception, not the rule. Most helicase modules in other DEAD-box proteins are modified, some by insertions into the RecA-like domains, and the majority by N- and C-terminal appendages. While the basic catalytic function resides within the helicase core, its modulation by insertions, additional domains or a network of interaction partners generates the diversity of DEAD-box protein functions in the cell. This review summarizes the current knowledge on eIF4A and its regulation, and discusses to what extent eIF4A serves as a model DEAD-box protein.
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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.