ArticleNature communications2016
Crystal structures of the human elongation factor eEFSec suggest a non-canonical mechanism for selenocysteine incorporation.
Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers, 1 of them a synthesis that pooled it.
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Who cites it
18 citing papers in PubMed, 1 synthesis or guideline pooled it, 35 citations in OpenAlex.
- Genetic risk of clozapine-induced leukopenia and neutropenia: a genome-wide association study.Translational psychiatry · 2021Pooled it
- Nutritional supplementation remodels yak cardiac molecular networks through selenoprotein activation and immune quiescence.Frontiers in nutrition · 2026Article
- Association between trace metal element levels and ideal cardiovascular health in adolescents.European journal of medical research · 2025Article
- Clinical and Genetic Factors Associated with Intraoperative Minimum Alveolar Concentration Ratio: A Single-center Retrospective Cohort and Genome-wide Association Study.Anesthesiology · 2025Article
- Identifying compound heterozygous variants in the EEFSEC gene linked to progressive cerebellar atrophy.Journal of neurodevelopmental disorders · 2025Article
- The origins and evolution of translation factors.Trends in genetics : TIG · 2025Review
- EEFSEC deficiency: A selenopathy with early-onset neurodegeneration.American journal of human genetics · 2025Article
- Identification of Potential Diagnostic Biomarkers and Drug Targets for Endometriosis from a Genetic Perspective: A Mendelian Randomization Study.Gynecologic and obstetric investigation · 2025Article
- PRDX6 augments selenium utilization to limit iron toxicity and ferroptosis.Nature structural & molecular biology · 2024Article
- Seryl-tRNA synthetase promotes translational readthrough by mRNA binding and involvement of the selenocysteine incorporation machinery.Nucleic acids research · 2023Article
- Association of rs142548867 (EEFSEC) and periodontitis Grade C in a young Brazilian population.Journal of applied oral science : revista FOB · 2023Article
- A Common Genetic Factor Underlies Genetic Risk for Gynaecological and Reproductive Disorders and Is Correlated with Risk to Depression.Neuroendocrinology · 2023Article
- Structure of the mammalian ribosome as it decodes the selenocysteine UGA codon.Science (New York, N.Y.) · 2022Article
- Ribosome Fate during Decoding of UGA-Sec Codons.International journal of molecular sciences · 2021Review
- Human Disorders Affecting the Selenocysteine Incorporation Pathway Cause Systemic Selenoprotein Deficiency.Antioxidants & redox signaling · 2020Article
- HOxidative medicine and cellular longevity · 2019Article
- On elongation factor eEFSec, its role and mechanism during selenium incorporation into nascent selenoproteins.Biochimica et biophysica acta. General subjects · 2018Review
- Computational identification of the selenocysteine tRNA (tRNASec) in genomes.PLoS computational biology · 2017Article
Corrections and comments
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Authors and funding
7 authors at 5 institutions in 1 country.
Funding
Abstract
Selenocysteine is the only proteinogenic amino acid encoded by a recoded in-frame UGA codon that does not operate as the canonical opal stop codon. A specialized translation elongation factor, eEFSec in eukaryotes and SelB in prokaryotes, promotes selenocysteine incorporation into selenoproteins by a still poorly understood mechanism. Our structural and biochemical results reveal that four domains of human eEFSec fold into a chalice-like structure that has similar binding affinities for GDP, GTP and other guanine nucleotides. Surprisingly, unlike in eEF1A and EF-Tu, the guanine nucleotide exchange does not cause a major conformational change in domain 1 of eEFSec, but instead induces a swing of domain 4. We propose that eEFSec employs a non-canonical mechanism involving the distinct C-terminal domain 4 for the release of the selenocysteinyl-tRNA during decoding on the ribosome.
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Registered trials
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