ArticleThe Journal of biological chemistry2017
Protein glutaminylation is a yeast-specific posttranslational modification of elongation factor 1A.
Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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
8 citing papers in PubMed, 14 citations in OpenAlex.
- Identification of the Relationship between Hub Genes and Immune Cell Infiltration in Vascular Endothelial Cells of Proliferative Diabetic Retinopathy Using Bioinformatics Methods.Disease markers · 2022Article
- Mutational analysis reveals potential phosphorylation sites in eukaryotic elongation factor 1A that are important for its activity.FEBS letters · 2021Article
- Screening Potential Reference Genes inGenes · 2021Article
- Evidence for a synergistic effect of post-translational modifications and genomic composition of eEF-1α on the adaptation ofEcology and evolution · 2021Article
- Protein Methylation and Translation: Role of Lysine Modification on the Function of Yeast Elongation Factor 1A.Biochemistry · 2019Article
- Sequencing the mosaic genome of Brahman cattle identifies historic and recent introgression including polled.Scientific reports · 2018Article
- Regulation of eukaryotic elongation factor 1 alpha (eEF1A) by dynamic lysine methylation.RNA biology · 2018Article
- Evaluation of Reference Genes for Real-Time Quantitative PCR Analysis in Larvae ofFrontiers in physiology · 2018Article
Corrections and comments
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Authors and funding
11 authors at 5 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ribosomal translation factors are fundamental for protein synthesis and highly conserved in all kingdoms of life. The essential eukaryotic elongation factor 1A (eEF1A) delivers aminoacyl tRNAs to the A-site of the translating 80S ribosome. Several studies have revealed that eEF1A is posttranslationally modified. Using MS analysis, site-directed mutagenesis, and X-ray structural data analysis of
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