ReviewInternational journal of molecular sciences2021
On the Need to Tell Apart Fraternal Twins eEF1A1 and eEF1A2, and Their Respective Outfits.
Review in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 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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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.
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Who cites it
24 citing papers in PubMed, 35 citations in OpenAlex.
- SARS-CoV-2 nucleocapsid protein hijacks host transcription by targeting eEF1A1.Life science alliance · 2026Article
- Identification of boholamide A analogue as a potential hypoxia-selective anti-triple-negative breast cancer agent by targeting eEF1A1.Acta pharmaceutica Sinica. B · 2026Article
- EEF1AKMT4-eEF1A2 synergistically facilitates the progression of GBC by promoting ribosomal protein output.Genes & diseases · 2026Article
- Dynamics and structural features of the eEF1A1 and eEF1A2 paralogs.Nucleic acids research · 2025Article
- The proteomic landscape of diffuse midline glioma highlights the therapeutic potential of non-histone protein methyltransferases.Neuro-oncology · 2025Article
- Targeting Eukaryotic Elongation Factor 1A: How Small-Molecule Inhibitors Suppress Tumor Growth via Diverse Pathways.International journal of molecular sciences · 2025Review
- Multidimensional Regulatory Mechanisms and Targeting Strategies of the eEF1 Family in RNA Virus Infection.Viruses · 2025Review
- Exploiting Translation Machinery for Cancer Therapy: Translation Factors as Promising Targets.International journal of molecular sciences · 2024Review
- N-Acetylcysteine Inhibits Coxsackievirus B3 Replication by Downregulating Eukaryotic Translation Elongation Factor 1 Alpha 1.Viruses · 2024Article
- Unmasking of molecular players: proteomic profiling of vitreous humor in pathologic myopia.BMC ophthalmology · 2024Observational
- Face-valid phenotypes in a mouse model of the most common mutation in EEF1A2-related neurodevelopmental disorder.Disease models & mechanisms · 2024Article
- MILIP Binding to tRNAs Promotes Protein Synthesis to Drive Triple-Negative Breast Cancer.Cancer research · 2024Article
- Oncogenic activation of EEF1A2 expression: a journey from a putative to an established oncogene.Cellular & molecular biology letters · 2024Review
- Genome-wide analysis of the soybeanFrontiers in plant science · 2024Article
- Article
- Anticancer Small-Molecule Agents Targeting Eukaryotic Elongation Factor 1A: State of the Art.International journal of molecular sciences · 2023Review
- Immune responses of different COVID-19 vaccination strategies by analyzing single-cell RNA sequencing data from multiple tissues using machine learning methods.Frontiers in genetics · 2023Article
- The eEF1 family of mammalian translation elongation factors.BBA advances · 2023Article
- Lipid-independent activation of a muscle-specific PKCα splicing variant.American journal of physiology. Heart and circulatory physiology · 2022Article
- Initiation and elongation factor co-expression correlates with recurrence and survival in epithelial ovarian cancer.Journal of ovarian research · 2022Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
eEF1A1 and eEF1A2 are paralogous proteins whose presence in most normal eukaryotic cells is mutually exclusive and developmentally regulated. Often described in the scientific literature under the collective name eEF1A, which stands for eukaryotic elongation factor 1A, their best known activity (in a monomeric, GTP-bound conformation) is to bind aminoacyl-tRNAs and deliver them to the A-site of the 80S ribosome. However, both eEF1A1 and eEF1A2 are endowed with multitasking abilities (sometimes performed by homo- and heterodimers) and can be located in different subcellular compartments, from the plasma membrane to the nucleus. Given the high sequence identity of these two sister proteins and the large number of post-translational modifications they can undergo, we are often confronted with the dilemma of discerning which is the particular proteoform that is actually responsible for the ascribed biochemical or cellular effects. We argue in this review that acquiring this knowledge is essential to help clarify, in molecular and structural terms, the mechanistic involvement of these two ancestral and abundant G proteins in a variety of fundamental cellular processes other than translation elongation. Of particular importance for this special issue is the fact that several de novo heterozygous missense mutations in the human
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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.