ArticleChemical science2022
Chemical synthesis of human selenoprotein F and elucidation of its thiol-disulfide oxidoreductase activity.
Article in Chemical science, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Article
- Bioinformatics identification and experimental validation of hub genes associated with narcolepsy type 1.Journal of clinical and translational science · 2026Article
- Advances in the chemical synthesis of human proteoforms.Science China. Life sciences · 2025Review
- Azole reagents enabled ligation of peptide acyl pyrazoles for chemical protein synthesis.Chemical science · 2024Article
- The semisynthesis of nucleolar human selenoprotein H.Chemical science · 2023Article
- Selenoprotein F Knockout Caused Glucose Metabolism Disorder in Young Mice by Disrupting Redox Homeostasis.Antioxidants (Basel, Switzerland) · 2022Article
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Authors and funding
3 authors.
Funding
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Abstract
Selenoprotein F (SelF) is an endoplasmic reticulum-residing eukaryotic protein that contains a selenocysteine (Sec) residue. It has been suggested to be involved in a number of physiological processes by acting as a thiol-disulfide oxidoreductase, but the exact role has remained unclear due to the lack of a reliable production method. We document herein a robust synthesis of the human SelF through a three-segment two-ligation semisynthesis strategy. Highlighted in this synthetic route are the use of a mild desulfurization process to protect the side-chain of the Sec residue from being affected and the simultaneous removal of acetamidomethyl and
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