ArticleStructure (London, England : 1993)2013
Dynamic recognition of the mRNA cap by Saccharomyces cerevisiae eIF4E.
Article in Structure (London, England : 1993), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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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.
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Who cites it
30 citing papers in PubMed, 47 citations in OpenAlex.
- SM-NucSeq, Genetic and Epigenetic Sequencing of Nucleosomes with Single-Molecule Real-Time Sequencing.Nano letters · 2026Article
- Eukaryotic translation initiation factor 4F: functional properties and physiological role.Nucleic acids research · 2025Review
- Dynamics and Regulation of mRNA Cap Recognition by Human eIF4F.bioRxiv : the preprint server for biology · 2025Article
- Sortase-Mediated Fluorescent Labeling of eIF4E for Investigating Translation Initiation Mechanisms.Biochemistry · 2025Article
- The mechanism of mRNA cap recognition.Nature · 2025Article
- Single-molecule tracking reveals dynamic regulation of ribosomal scanning.Science advances · 2024Article
- Depletion of cap-binding protein eIF4E dysregulates amino acid metabolic gene expression.Molecular cell · 2024Article
- The mechanism of mRNA activation.bioRxiv : the preprint server for biology · 2023Article
- Single-molecule visualization of mRNA circularization during translation.Experimental & molecular medicine · 2023Review
- mRNA- and factor-driven dynamic variability controls eIF4F-cap recognition for translation initiation.Nucleic acids research · 2022Article
- Bayesian machine learning analysis of single-molecule fluorescence colocalization images.eLife · 2022Article
- The flip-flop configuration of the PABP-dimer leads to switching of the translation function.Nucleic acids research · 2022Article
- Smart-ORF: a single-molecule method for accessing ribosome dynamics in both upstream and main open reading frames.Nucleic acids research · 2021Article
- Heterogeneous Dynamics of Protein-RNA Interactions across Transcriptome-Derived Messenger RNA Populations.Journal of the American Chemical Society · 2020Article
- An in vitro single-molecule assay for eukaryotic cap-dependent translation initiation kinetics.Nucleic acids research · 2020Article
- Article
- Protein Synthesis Initiation in Eukaryotic Cells.Cold Spring Harbor perspectives in biology · 2018Review
- Article
- Properties of the ternary complex formed by yeast eIF4E, p20 and mRNA.Scientific reports · 2018Article
- Dynamic changes in eIF4F-mRNA interactions revealed by global analyses of environmental stress responses.Genome biology · 2017Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Recognition of the mRNA 5' m⁷G(5')ppp(5')N cap is key to translation initiation for most eukaryotic mRNAs. The cap is bound by the eIF4F complex, consisting of a cap-binding protein (eIF4E), a "scaffold" protein (eIF4G), and an RNA helicase (eIF4A). As a central early step in initiation, regulation of eIF4F is crucial for cellular viability. Although the structure and function of eIF4E have been defined, a dynamic mechanistic picture of its activity at the molecular level in the eIF4F·mRNA complex is still unavailable. Here, using single-molecule fluorescence, we measured the effects of Saccharomyces cerevisiae eIF4F factors, mRNA secondary structure, and the poly(A)-binding protein Pab1p on eIF4E-mRNA binding dynamics. Our data provide an integrated picture of how eIF4G and mRNA structure modulate eIF4E-mRNA interaction, and uncover an eIF4G- and poly(A)-independent activity of poly(A)-binding protein that prolongs the eIF4E·mRNA complex lifetime.
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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.