ArticleNucleic acids research2016
Structure of the hypusinylated eukaryotic translation factor eIF-5A bound to the ribosome.
Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 97 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
97 citing papers in PubMed, 137 citations in OpenAlex.
- Halting translation by the letter with sequence-selective small molecules.Nature chemical biology · 2026Review
- eIF5A and polyamines restrict mRNA levels in response to ribosome stalls.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Gut‑bone metabolites: SCFAs, polyamines and microbial metabolomics in osteoporosis risk and therapy (Review).International journal of molecular medicine · 2026Review
- Spermidine in Colorectal cancer: friend or foe?Amino acids · 2026Review
- SNOR promotes translation restart after dormancy.Nature · 2026Article
- rRNA expansion segments mediate ribosome dimerization as a conserved stress response.Nucleic acids research · 2026Article
- Adaptive crosstalk between polyamine metabolism, translation, and autophagy sustains energy homeostasis in mammals during starvation: a scoping review.Amino acids · 2026Review
- A Novel Eukaryotic Ribosome Factor Enables Translation Restart Following Cellular Dormancy.bioRxiv : the preprint server for biology · 2026Article
- The role of spermidine in plants and humans: a pathway from climate change adaptation to health benefits.NPJ science of food · 2026Review
- Structural basis of TACO1-mediated efficient mitochondrial translation.Nature communications · 2026Article
- Constant trouble with prolines-navigating a global translation dilemma.Nucleic acids research · 2026Review
- Crystallographic fragment screening supports tool compound discovery and reveals conformational flexibility in human deoxyhypusine synthase.Communications chemistry · 2026Article
- Mechanical forces regulate the composition and fate of stalled nascent chains.Molecular cell · 2026Article
- Full-protein release assay in a reconstituted yeast translation system using GGQ-methylated eRF1.Frontiers in molecular biosciences · 2026Article
- Structural Basis of TACO1-Mediated Efficient Mitochondrial Translation.bioRxiv : the preprint server for biology · 2025Article
- Synergistic Methods to Investigate Eukaryotic Translation and Its Quality Control.Journal of molecular biology · 2025Review
- Translational regulation in stress biology.Nature cell biology · 2025Review
- The generation and consequences of N-terminal proteoform diversity.Cell reports · 2025Review
- Emerging mechanisms of human mitochondrial translation regulation.Trends in biochemical sciences · 2025Review
- The assembly factor Reh1 is released from the ribosome during its initial round of translation.Nature communications · 2025Article
37 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
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
During protein synthesis, ribosomes become stalled on polyproline-containing sequences, unless they are rescued in archaea and eukaryotes by the initiation factor 5A (a/eIF-5A) and in bacteria by the homologous protein EF-P. While a structure of EF-P bound to the 70S ribosome exists, structural insight into eIF-5A on the 80S ribosome has been lacking. Here we present a cryo-electron microscopy reconstruction of eIF-5A bound to the yeast 80S ribosome at 3.9 Å resolution. The structure reveals that the unique and functionally essential post-translational hypusine modification reaches toward the peptidyltransferase center of the ribosome, where the hypusine moiety contacts A76 of the CCA-end of the P-site tRNA. These findings would support a model whereby eIF-5A stimulates peptide bond formation on polyproline-stalled ribosomes by stabilizing and orienting the CCA-end of the P-tRNA, rather than by directly contributing to the catalysis.
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.