ArticleNucleic acids research2013
UGA codon position-dependent incorporation of selenocysteine into mammalian selenoproteins.
Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 36 citations in OpenAlex.
- Oxidative stress in pigs and opportunities with selenium-containing amino acids.Stress biology · 2026Review
- 3S-DB identifies an RNA repository facilitating stop codon readthrough for selenocysteine insertion and selenoproteome expansion.Redox biology · 2025Article
- Selenium and selenoproteins: key regulators of ferroptosis and therapeutic targets in cancer.Journal of molecular medicine (Berlin, Germany) · 2025Review
- Type I Iodothyronine Deiodinase Functions in Thyroid Hormone Synthesis and Growth Regulation in Bivalve.Marine biotechnology (New York, N.Y.) · 2025Article
- Improving Catalytic Activity, Acid-Tolerance, and Thermal Stability of Glutathione Peroxidase by Systematic Site-Directed Selenocysteine Incorporation.Molecular biotechnology · 2023Article
- Ribosome Fate during Decoding of UGA-Sec Codons.International journal of molecular sciences · 2021Review
- Pathogenic Variants in Selenoproteins and Selenocysteine Biosynthesis Machinery.International journal of molecular sciences · 2021Review
- An Ancient Clade of Penelope-Like Retroelements with Permuted Domains Is Present in the Green Lineage and Protists, and Dominates Many Invertebrate Genomes.Molecular biology and evolution · 2021Article
- SECISBP2 is a novel prognostic predictor that regulates selenoproteins in diffuse large B-cell lymphoma.Laboratory investigation; a journal of technical methods and pathology · 2021Article
- Tolerance to Selenoprotein Loss Differs between Human and Mouse.Molecular biology and evolution · 2020Article
- Identification of the Selenoprotein S Positive UGA Recoding (SPUR) element and its position-dependent activity.RNA biology · 2019Article
- New Directions for Understanding the Codon Redefinition Required for Selenocysteine Incorporation.Biological trace element research · 2019Review
- Acetylation Regulates Thioredoxin Reductase Oligomerization and Activity.Antioxidants & redox signaling · 2018Article
- Latest development on RNA-based drugs and vaccines.Future science OA · 2018Review
- Stable and Potent Selenomab-Drug Conjugates.Cell chemical biology · 2017Article
- Human selenoprotein P and S variant mRNAs with different numbers of SECIS elements and inferences from mutant mice of the roles of multiple SECIS elements.Open biology · 2016Article
- Selenium in the Therapy of Neurological Diseases. Where is it Going?Current neuropharmacology · 2016Review
- Regulation of selenocysteine incorporation into the selenium transport protein, selenoprotein P.The Journal of biological chemistry · 2014Article
- Selenoproteins: molecular pathways and physiological roles.Physiological reviews · 2014Review
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
It is thought that the SelenoCysteine Insertion Sequence (SECIS) element and UGA codon are sufficient for selenocysteine (Sec) insertion. However, we found that UGA supported Sec insertion only at its natural position or in its close proximity in mammalian thioredoxin reductase 1 (TR1). In contrast, Sec could be inserted at any tested position in mammalian TR3. Replacement of the 3'-UTR of TR3 with the corresponding segment of a Euplotes crassus TR restricted Sec insertion into the C-terminal region, whereas the 3'-UTR of TR3 conferred unrestricted Sec insertion into E. crassus TR, in which Sec insertion is normally limited to the C-terminal region. Exchanges of 3'-UTRs between mammalian TR1 and E. crassus TR had no effect, as both proteins restricted Sec insertion. We further found that these effects could be explained by the use of selenoprotein-specific SECIS elements. Examination of Sec insertion into other selenoproteins was consistent with this model. The data indicate that mammals evolved the ability to limit Sec insertion into natural positions within selenoproteins, but do so in a selenoprotein-specific manner, and that this process is controlled by the SECIS element in the 3'-UTR.
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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.