ArticleThe Journal of biological chemistry2007
Kinetics of the interactions between yeast elongation factors 1A and 1Balpha, guanine nucleotides, and aminoacyl-tRNA.
Article in The Journal of biological chemistry, 2007. 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, 43 citations in OpenAlex.
- Cryo-EM structure of the human MON1A-CCZ1-RAB7A complex provides insights into nucleotide exchange mechanism.Life metabolism · 2025Article
- The origins and evolution of translation factors.Trends in genetics : TIG · 2025Review
- Assay for ribosome stimulation of angiogenin nuclease activity.Methods in enzymology · 2025Article
- Article
- Genome-wide analysis of the soybeanFrontiers in plant science · 2024Article
- Mutational analysis reveals potential phosphorylation sites in eukaryotic elongation factor 1A that are important for its activity.FEBS letters · 2021Article
- Therapeutic promise of engineered nonsense suppressor tRNAs.Wiley interdisciplinary reviews. RNA · 2021Review
- Functions and Regulation of Translation Elongation Factors.Frontiers in molecular biosciences · 2021Review
- In Silico Structural Modeling and Analysis of Elongation Factor-1 Alpha and Elongation Factor-like Protein.ACS omega · 2019Article
- Functions of unconventional mammalian translational GTPases GTPBP1 and GTPBP2.Genes & development · 2018Article
- Translation Elongation and Recoding in Eukaryotes.Cold Spring Harbor perspectives in biology · 2018Review
- Lack of 2'-O-methylation in the tRNA anticodon loop of two phylogenetically distant yeast species activates the general amino acid control pathway.PLoS genetics · 2018Article
- Fail-safe control of translation initiation by dissociation of eIF2α phosphorylated ternary complexes.eLife · 2017Article
- The C-terminal Helix of Pseudomonas aeruginosa Elongation Factor Ts Tunes EF-Tu Dynamics to Modulate Nucleotide Exchange.The Journal of biological chemistry · 2016Article
- Review: Translational GTPases.Biopolymers · 2016Review
- Analysis of Translation Elongation Dynamics in the Context of an Escherichia coli Cell.Biophysical journal · 2016Article
- Article
- Mammalian translation elongation factor eEF1A2: X-ray structure and new features of GDP/GTP exchange mechanism in higher eukaryotes.Nucleic acids research · 2014Article
- An evolutionary ratchet leading to loss of elongation factors in eukaryotes.BMC evolutionary biology · 2014Article
- The molecular biology of selenocysteine.Biomolecular concepts · 2013Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
Abstract
The interactions of elongation factor 1A (eEF1A) from Saccharomyces cerevisiae with elongation factor 1Balpha (eEF1Balpha), guanine nucleotides, and aminoacyl-tRNA were studied kinetically by fluorescence stopped-flow. eEF1A has similar affinities for GDP and GTP, 0.4 and 1.1 microm, respectively. Dissociation of nucleotides from eEF1A in the absence of the guanine nucleotide exchange factor is slow (about 0.1 s(-1)) and is accelerated by eEF1Balpha by 320-fold and 250-fold for GDP and GTP, respectively. The rate constant of eEF1Balpha binding to eEF1A (10(7)-10(8) M (-1) s(-1)) is independent of guanine nucleotides. At the concentrations of nucleotides and factors prevailing in the cell, the overall exchange rate is expected to be in the range of 6 s(-1), which is compatible with the rate of protein synthesis in the cell. eEF1A.GTP binds Phe-tRNA(Phe) with a K(d) of 3 nm, whereas eEF1A.GDP shows no significant binding, indicating that eEF1A has similar tRNA binding properties as its prokaryotic homolog, EF-Tu.
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.