ArticleNucleic acids research2014
Molecular insights into the interaction of the ribosomal stalk protein with elongation factor 1α.
Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. 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, 38 citations in OpenAlex.
- Ribosomal allostery as a potential regulator of bacterial dormancy.Nature communications · 2026Article
- Structural mechanism of mRNA decoding by mammalian GTPase GTPBP1.Nature communications · 2025Article
- Structural mechanism of mRNA decoding by mammalian GTPase GTPBP1.bioRxiv : the preprint server for biology · 2025Article
- The origins and evolution of translation factors.Trends in genetics : TIG · 2025Review
- eEF2K regulates pain through translational control of BDNF.Molecular cell · 2025Article
- Reference genes for qPCR expression in black tiger shrimp, Penaeus monodon.Molecular biology reports · 2024Article
- Proteomic screening identifies RPLp2 as a specific regulator for the translation of coronavirus.International journal of biological macromolecules · 2023Article
- Archaea/eukaryote-specific ribosomal proteins - guardians of a complex structure.Computational and structural biotechnology journal · 2023Review
- Nsun4 and Mettl3 mediated translational reprogramming of Sox9 promotes BMSC chondrogenic differentiation.Communications biology · 2022Article
- Impact of Genome Reduction in Microsporidia.Experientia supplementum (2012) · 2022Article
- Direct visualization of translational GTPase factor pool formed around the archaeal ribosomal P-stalk by high-speed AFM.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Structural basis for the interaction of Shiga toxin 2a with a C-terminal peptide of ribosomal P stalk proteins.The Journal of biological chemistry · 2020Article
- Ribosomal stress-surveillance: three pathways is a magic number.Nucleic acids research · 2020Review
- Slowing ribosome velocity restores folding and function of mutant CFTR.The Journal of clinical investigation · 2019Article
- Towards a model of GCN2 activation.Biochemical Society transactions · 2019Review
- Switch of the interactions between the ribosomal stalk and EF1A in the GTP- and GDP-bound conformations.Scientific reports · 2019Article
- How Ricin Damages the Ribosome.Toxins · 2019Review
- Peptide Mimics of the Ribosomal P Stalk Inhibit the Activity of Ricin A Chain by Preventing Ribosome Binding.Toxins · 2018Article
- The ribosomal stalk protein is crucial for the action of the conserved ATPase ABCE1.Nucleic acids research · 2018Article
- Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In all organisms, the large ribosomal subunit contains multiple copies of a flexible protein, the so-called 'stalk'. The C-terminal domain (CTD) of the stalk interacts directly with the translational GTPase factors, and this interaction is required for factor-dependent activity on the ribosome. Here we have determined the structure of a complex of the CTD of the archaeal stalk protein aP1 and the GDP-bound archaeal elongation factor aEF1α at 2.3 Å resolution. The structure showed that the CTD of aP1 formed a long extended α-helix, which bound to a cleft between domains 1 and 3 of aEF1α, and bridged these domains. This binding between the CTD of aP1 and the aEF1α•GDP complex was formed mainly by hydrophobic interactions. The docking analysis showed that the CTD of aP1 can bind to aEF1α•GDP located on the ribosome. An additional biochemical assay demonstrated that the CTD of aP1 also bound to the aEF1α•GTP•aminoacyl-tRNA complex. These results suggest that the CTD of aP1 interacts with aEF1α at various stages in translation. Furthermore, phylogenetic perspectives and functional analyses suggested that the eukaryotic stalk protein also interacts directly with domains 1 and 3 of eEF1α, in a manner similar to the interaction of archaeal aP1 with aEF1α.
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.