ArticleMethods in enzymology2022
Identification of selenoprotein O substrates using a biotinylated ATP analog.
Article in Methods in enzymology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 7 citations in OpenAlex.
- Selenium Deficiency is a Significant Risk Factor for Sarcopenia: Evidence and Selenoprotein-Mediated Mechanisms.Biological trace element research · 2026Review
- Selenoproteins: Minute yet vital players governing cellular fate.Genes & diseases · 2026Review
- A repurposed AMP binding domain reveals mitochondrial protein AMPylation as a regulator of cellular metabolism.Nature communications · 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
- Selenoprotein O Promotes Melanoma Metastasis and Regulates Mitochondrial Complex II Activity.Cancer research · 2025Article
- Utilizing Thermal Shift Assay to Probe Substrate Binding to Selenoprotein O.Journal of visualized experiments : JoVE · 2024Article
- Selenoproteins and the senescence-associated epitranscriptome.Experimental biology and medicine (Maywood, N.J.) · 2022Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Selenoprotein O is one of 25 human selenoproteins that incorporate the 21st amino acid selenocysteine. Recent studies have revealed a previously undocumented mechanism of redox regulation by which SelO protects cells from oxidative damage. SelO catalyzes the covalent addition of AMP from ATP to the hydroxyl side chain of protein substrates in a post translational modification known as AMPylation. Although AMPylation was discovered over 50 years ago, methods to detect and enrich substrates are limited. Here, we describe protocols to clone, purify, and identify the substrates of bacterial SelO using a biotinylated ATP analog. Identification of SelO substrates and the functional consequences of AMPylation will illuminate the significance of this evolutionarily conserved selenoprotein.
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