ReviewInternational journal of molecular sciences2023
Biological and Catalytic Properties of Selenoproteins.
Review in International journal of molecular sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers, 1 of them a synthesis that pooled it.
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
26 citing papers in PubMed, 1 synthesis or guideline pooled it, 45 citations in OpenAlex.
- Associations of selenium status with all-cause and cause-specific mortality: a systematic review and meta-analysis of cohort studies.Redox biology · 2025Pooled it
- From water to land: evolution of tRNA gene repertoires in photosynthetic organisms.The EMBO journal · 2026Review
- Selenium: From Redox Signaling to Interactions with the Gut Microbiome.Biological trace element research · 2026Review
- Selenotrisulfide delivery restores redox balance in myocardial infarction via a thiol-exchange reactionBioactive materials · 2026Article
- Synergistic Effects of Selenium, Selenoproteins, Selenocysteine and Procyanidin A2 Based on Immune Response and Oxidative Stress.Molecules (Basel, Switzerland) · 2026Review
- Anti-Aging Potential of Biogenic Selenium Nanoparticles and Selenium/Polysaccharides Nanoconjugate Biosynthesized byAntioxidants (Basel, Switzerland) · 2026Article
- Evaluation of the Variability in Selenoprotein Genes in Hepatocellular Carcinoma Patients.Biochemical genetics · 2026Article
- Recent advances in exploring the composition and evolution of the prokaryotic selenoproteome.Applied and environmental microbiology · 2026Review
- BSepDB: a database of bacterial selenoprotein genes and proteins.BMC genomics · 2026Article
- Replacing of Cysteine with Selenocysteine: Biochemical Considerations, Computational Modeling, and Protein Engineering Applications.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Novel nutraceutical combination restores hepatic deiodinase expression and protein levels under inflammatory conditions: evidence from anFrontiers in nutrition · 2026Article
- Selenoprotein S and the Causal Risk of Hypertension in Pregnancy: A Mendelian Randomization Study.Healthcare (Basel, Switzerland) · 2025Article
- Exploring the Antioxidant Roles of Cysteine and Selenocysteine in Cellular Aging and Redox Regulation.Biomolecules · 2025Review
- deep-Sep: a deep learning-based method for fast and accurate prediction of selenoprotein genes in bacteria.mSystems · 2025Article
- Article
- Interaction of Heavy Metals (Cadmium and Selenium) in an Experimental Study on Goldfish: Hematobiochemical Changes and Oxidative Stress.Journal of xenobiotics · 2025Article
- The Promising Role of Selenium and Yeast in the Fight Against Protein Amyloidosis.Biological trace element research · 2025Review
- Genetically Elevated Selenoprotein S Levels and Risk of Stroke: A Two-Sample Mendelian Randomization Analysis.International journal of molecular sciences · 2025Article
- Selenium and Selenoproteins: Mechanisms, Health Functions, and Emerging Applications.Molecules (Basel, Switzerland) · 2025Review
- Increased Expression of PHGDH Under High-Selenium Stress In Vivo.Biological trace element research · 2024Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Selenocysteine is a catalytic residue at the active site of all selenoenzymes in bacteria and mammals, and it is incorporated into the polypeptide backbone by a co-translational process that relies on the recoding of a UGA termination codon into a serine/selenocysteine codon. The best-characterized selenoproteins from mammalian species and bacteria are discussed with emphasis on their biological function and catalytic mechanisms. A total of 25 genes coding for selenoproteins have been identified in the genome of mammals. Unlike the selenoenzymes of anaerobic bacteria, most mammalian selenoenzymes work as antioxidants and as redox regulators of cell metabolism and functions. Selenoprotein P contains several selenocysteine residues and serves as a selenocysteine reservoir for other selenoproteins in mammals. Although extensively studied, glutathione peroxidases are incompletely understood in terms of local and time-dependent distribution, and regulatory functions. Selenoenzymes take advantage of the nucleophilic reactivity of the selenolate form of selenocysteine. It is used with peroxides and their by-products such as disulfides and sulfoxides, but also with iodine in iodinated phenolic substrates. This results in the formation of Se-X bonds (X = O, S, N, or I) from which a selenenylsulfide intermediate is invariably produced. The initial selenolate group is then recycled by thiol addition. In bacterial glycine reductase and D-proline reductase, an unusual catalytic rupture of selenium-carbon bonds is observed. The exchange of selenium for sulfur in selenoproteins, and information obtained from model reactions, suggest that a generic advantage of selenium compared with sulfur relies on faster kinetics and better reversibility of its oxidation reactions.
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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.