ArticleMethods in molecular biology (Clifton, N.J.)2018
Selenocysteine-Mediated Expressed Protein Ligation of SELENOM.
Article in Methods in molecular biology (Clifton, N.J.), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 14 citations in OpenAlex.
- Advances in the chemical synthesis of human proteoforms.Science China. Life sciences · 2025Review
- Intein-based Design Expands Diversity of Selenocysteine Reporters.Journal of molecular biology · 2022Article
- Chemical Biology Approaches to Interrogate the Selenoproteome.Accounts of chemical research · 2019Review
- Synthesis and semisynthesis of selenopeptides and selenoproteins.Current opinion in chemical biology · 2018Review
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3 authors at 1 institution in 1 country.
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Abstract
A sizeable fraction of the selenoproteome encodes oxidoreductases possessing a thioredoxin fold, a structural motif that is shared among a diverse group of enzymes. In these oxidoreductases, the active site is comprised of a cysteine and a selenocysteine separated by one to two amino acids. In a subset of these selenoproteins, such as human SELENOH, SELENOM, SELENOT, SELENOV, SELENOW, and SELENOF, this redox motif is positioned immediately after the first β-sheet in a short loop, and is essential for interactions with its substrate or partners. Here, we describe the preparation of a representative member of this group, SELENOM, by selenocysteine-driven expressed protein ligation. The preparation employs a peptide bond formation between two protein fragments expressed recombinantly in E. coli. This method can be employed to prepare other selenoproteins.
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