ArticleNucleic acids research2014
eIF5 and eIF5B together stimulate 48S initiation complex formation during ribosomal scanning.
Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It carries an expression of concern. Cited by 31 papers.
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.
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
31 citing papers in PubMed, 51 citations in OpenAlex.
- Article
- Synergistic Methods to Investigate Eukaryotic Translation and Its Quality Control.Journal of molecular biology · 2025Review
- eIF1 and eIF5 dynamically control translation start site fidelity.Nature structural & molecular biology · 2025Article
- Exploring the interaction dynamics of eukaryotic translation initiation factor 2.Biochemical Society transactions · 2025Review
- Remodelled ribosomal populations synthesize a specific proteome in proliferating plant tissue during cold.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025Article
- Eukaryotic initiation factors: central factor associating mRNA translational plasticity during neuropathic pain progression.Frontiers in neurology · 2025Review
- The dark side of mRNA translation and the translation machinery in glioblastoma.Frontiers in cell and developmental biology · 2023Review
- Article
- Conformational rearrangements upon start codon recognition in human 48S translation initiation complex.Nucleic acids research · 2022Article
- Translation initiation and its relevance in colorectal cancer.The FEBS journal · 2021Review
- eIF5 and eIF5B together stimulate 48S initiation complex formation during ribosomal scanning.Nucleic acids research · 2021Article
- KRASInternational journal of molecular sciences · 2021Article
- Established and Emerging Regulatory Roles of Eukaryotic Translation Initiation Factor 5B (eIF5B).Frontiers in genetics · 2021Review
- Translation Regulation by eIF2α Phosphorylation and mTORC1 Signaling Pathways in Non-Communicable Diseases (NCDs).International journal of molecular sciences · 2020Review
- Long-range interdomain communications in eIF5B regulate GTP hydrolysis and translation initiation.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Migration of Small Ribosomal Subunits on the 5' Untranslated Regions of Capped Messenger RNA.International journal of molecular sciences · 2019Article
- Article
- DDX3X and specific initiation factors modulate FMR1 repeat-associated non-AUG-initiated translation.EMBO reports · 2019Article
- eIF4B and eIF4H mediate GR production from expanded G4C2 in a Drosophila model for C9orf72-associated ALS.Acta neuropathologica communications · 2019Article
- Protein Synthesis Initiation in Eukaryotic Cells.Cold Spring Harbor perspectives in biology · 2018Review
Corrections and comments
- Expression of concern
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
48S initiation complex (48S IC) formation is the first stage in the eukaryotic translation process. According to the canonical mechanism, 40S ribosomal subunit binds to the 5'-end of messenger RNA (mRNA) and scans its 5'-untranslated region (5'-UTR) to the initiation codon where it forms the 48S IC. Entire process is mediated by initiation factors. Here we show that eIF5 and eIF5B together stimulate 48S IC formation influencing initiation codon selection during ribosomal scanning. Initiation on non-optimal start codons--following structured 5'-UTRs, in bad AUG context, within few nucleotides from 5'-end of mRNA and CUG start codon--is the most affected. eIF5-induced hydrolysis of eIF2-bound GTP is essential for stimulation. GTP hydrolysis increases the probability that scanning ribosomal complexes will recognize and arrest scanning at a non-optimal initiation codon. Such 48S ICs are less stable owing to dissociation of eIF2*GDP from initiator tRNA, and eIF5B is then required to stabilize the initiator tRNA in the P site of 40S subunit. Alternative model that eIF5 and eIF5B cause 43S pre-initiation complex rearrangement favoring more efficient initiation codon recognition during ribosomal scanning is equally possible. Mutational analysis of eIF1A and eIF5B revealed distinct functions of eIF5B in 48S IC formation and subunit joining.
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.