ArticleBiochemistry2013
Contribution of selenocysteine to the peroxidase activity of selenoprotein S.
Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 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.
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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
23 citing papers in PubMed, 41 citations in OpenAlex.
- A Crystalline and Thermally Stable Selenocysteine Selenenic Acid.Angewandte Chemie (International ed. in English) · 2026Article
- Current views on selenoprotein S in the pathophysiological processes of diabetes-induced atherosclerosis: potential therapeutics and underlying biomarkers.Diabetology & metabolic syndrome · 2024Review
- Demonstration of the Formation of a Selenocysteine Selenenic Acid through Hydrolysis of a Selenocysteine Selenenyl Iodide Utilizing a Protective Molecular Cradle.Molecules (Basel, Switzerland) · 2023Article
- "Alphabet" Selenoproteins: Their Characteristics and Physiological Roles.International journal of molecular sciences · 2023Review
- Biological and Catalytic Properties of Selenoproteins.International journal of molecular sciences · 2023Review
- Selenoprotein S Interacts with the Replication and Transcription Complex of SARS-CoV-2 by Binding nsp7.Journal of molecular biology · 2023Article
- Noncanonical Form of ERAD Regulates Cardiac Hypertrophy.Circulation · 2023Article
- Selenoprotein S: A versatile disordered protein.Archives of biochemistry and biophysics · 2022Review
- Applying selenocysteine-mediated expressed protein ligation to prepare the membrane enzyme selenoprotein S.Methods in enzymology · 2022Article
- Diversity roles of CHD1L in normal cell function and tumorigenesis.Biomarker research · 2021Review
- Cul5-type Ubiquitin Ligase KLHDC1 Contributes to the Elimination of Truncated SELENOS Produced by Failed UGA/Sec Decoding.iScience · 2020Article
- Efficient Generation of Hydrazides in Proteins by RadA Split Intein.Chembiochem : a European journal of chemical biology · 2020Article
- Identification of the Selenoprotein S Positive UGA Recoding (SPUR) element and its position-dependent activity.RNA biology · 2019Article
- 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
- Differential regulation of cellular stress responses by the endoplasmic reticulum-resident Selenoprotein S (Seps1) in proliferating myoblasts versus myotubes.Physiological reports · 2018Article
- 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 S-dependent Selenoprotein K Binding to p97(VCP) Protein Is Essential for Endoplasmic Reticulum-associated Degradation.The Journal of biological chemistry · 2015Article
- Glutathione peroxidase's reaction intermediate selenenic acid is stabilized by the protein microenvironment.Free radical biology & medicine · 2014Article
- Selenoprotein K form an intermolecular diselenide bond with unusually high redox potential.FEBS letters · 2014Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Selenoprotein S (SelS, VIMP) is an intrinsically disordered enzyme that utilizes selenocysteine to catalyze the reduction of disulfide bonds and peroxides. Here it is demonstrated that selenocysteine is the residue oxidized by the peroxide substrate. It is possible to trap the reaction intermediate selenenic acid when the resolving cysteine is mutated. The selenocysteine allows SelS to rapidly re-form its selenenylsulfide bond following its reduction, and to resist inactivation by H2O2. We propose that SelS's peroxidase mechanism is similar to that of atypical 2-Cys peroxiredoxin and that selenocysteine allows SelS to sustain activity under oxidative stress.
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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 Socratic graph.