ArticleFEBS letters2014
Selenoprotein K form an intermolecular diselenide bond with unusually high redox potential.
Article in FEBS letters, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
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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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
18 citing papers in PubMed, 46 citations in OpenAlex.
- A Crystalline and Thermally Stable Selenocysteine Selenenic Acid.Angewandte Chemie (International ed. in English) · 2026Article
- Selenoprotein K Is a Peripheral ER Membrane Protein.Biochemistry · 2025Article
- Selenoprotein K at the intersection of cellular pathways.Archives of biochemistry and biophysics · 2025Review
- Selenoprotein S: A versatile disordered protein.Archives of biochemistry and biophysics · 2022Review
- Selenoprotein K protects skeletal muscle from damage and is required for satellite cells-mediated myogenic differentiation.Redox biology · 2022Article
- Integrated Analysis to Study the Relationship between Tumor-Associated Selenoproteins: Focus on Prostate Cancer.International journal of molecular sciences · 2020Article
- Efficient Generation of Hydrazides in Proteins by RadA Split Intein.Chembiochem : a European journal of chemical biology · 2020Article
- Molecular Mechanisms by Which Selenoprotein K Regulates Immunity and Cancer.Biological trace element research · 2019Review
- Progress in the emerging role of selenoproteins in cardiovascular disease: focus on endoplasmic reticulum-resident selenoproteins.Cellular and molecular life sciences : CMLS · 2019Review
- Can dimedone be used to study selenoproteins? An investigation into the reactivity of dimedone toward oxidized forms of selenocysteine.Protein science : a publication of the Protein Society · 2019Article
- Synthesis and semisynthesis of selenopeptides and selenoproteins.Current opinion in chemical biology · 2018Review
- Endoplasmic reticulum-resident selenoproteins as regulators of calcium signaling and homeostasis.Cell calcium · 2018Review
- Preparation of Selenocysteine-Containing Forms of Human SELENOK and SELENOS.Methods in molecular biology (Clifton, N.J.) · 2018Article
- Selenoprotein K Increases Efficiency of DHHC6 Catalyzed Protein Palmitoylation by Stabilizing the Acyl-DHHC6 Intermediate.Antioxidants (Basel, Switzerland) · 2017Article
- Quantification of Membrane Protein-Detergent Complex Interactions.The journal of physical chemistry. B · 2017Article
- Article
- Selenoprotein K and protein palmitoylation.Antioxidants & redox signaling · 2015Review
- (77)Se chemical shift tensor of L-selenocystine: experimental NMR measurements and quantum chemical investigations of structural effects.The journal of physical chemistry. B · 2015Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Selenoprotein K (SelK) is a membrane protein involved in antioxidant defense, calcium regulation and the ER-associated protein degradation pathway. We found that SelK exhibits a peroxidase activity with a rate that is low but within the range of other peroxidases. Notably, SelK reduced hydrophobic substrates, such as phospholipid hydroperoxides, which damage membranes. Thus, SelK might be involved in membrane repair or related pathways. SelK was also found to contain a diselenide bond-the first intramolecular bond of that kind reported for a selenoprotein. The redox potential of SelK was -257 mV, significantly higher than that of diselenide bonds in small molecules or proteins. Consequently, SelK can be reduced by thioredoxin reductase. These finding are essential for understanding SelK activity and function.
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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.