ArticleThe Journal of biological chemistry2018
Processive incorporation of multiple selenocysteine residues is driven by a novel feature of the selenocysteine insertion sequence.
Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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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
11 citing papers in PubMed, 14 citations in OpenAlex.
- Selenoproteins: Minute yet vital players governing cellular fate.Genes & diseases · 2026Review
- Design of synthetic selenopeptides with antioxidant activity for the treatment of XP and non-melanoma skin cancer.Frontiers in systems biology · 2026Article
- New-onset autoantibodies to selenoprotein P following severe burn injury.Frontiers in immunology · 2024Article
- Elovanoid-N34 modulates TXNRD1 key in protection against oxidative stress-related diseases.Cell death & disease · 2023Article
- The selenoprotein P 3' untranslated region is an RNA binding protein platform that fine tunes selenocysteine incorporation.PloS one · 2022Article
- Ribosome Fate during Decoding of UGA-Sec Codons.International journal of molecular sciences · 2021Review
- Mechanisms Affecting the Biosynthesis and Incorporation Rate of Selenocysteine.Molecules (Basel, Switzerland) · 2021Review
- Identification of a novel endogenous long non-coding RNA that inhibits selenoprotein P translation.Nucleic acids research · 2021Article
- Article
- Processive Recoding and Metazoan Evolution of Selenoprotein P: Up to 132 UGAs in Molluscs.Journal of molecular biology · 2019Article
- New Directions for Understanding the Codon Redefinition Required for Selenocysteine Incorporation.Biological trace element research · 2019Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
RNA stem loop structures have been frequently shown to regulate essential cellular processes. The selenocysteine insertion sequence (SECIS) element, found in the 3' UTRs of all selenoprotein mRNAs, is an example of such a structure, as it is required for the incorporation of the 21st amino acid, selenocysteine (Sec). Selenoprotein synthesis poses a mechanistic challenge because Sec is incorporated during translation in response to a stop codon (UGA). Although it is known that a SECIS-binding protein (SBP2) is required for Sec insertion, the mechanism of action remains elusive. Additional complexity is present in the synthesis of selenoprotein P (SELENOP), which is the only selenoprotein that contains multiple UGA codons and possesses two SECIS elements in its 3' UTR. Thus, full-length SELENOP synthesis requires processive Sec incorporation. Using zebrafish Selenop,
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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.