ArticleACS chemical biology2020
Generation of Recombinant Mammalian Selenoproteins through Genetic Code Expansion with Photocaged Selenocysteine.
Article in ACS chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 31 citations in OpenAlex.
- Site-Specific Protein Bioconjugation Through Cellular Incorporation of Noncanonical Amino Acids.Angewandte Chemie (International ed. in English) · 2026Review
- Optimized Directed Evolution of E. coli leucyl-tRNA Synthetase adds many Noncanonical Amino Acids into the Eukaryotic Genetic Code Including Ornithine and NAngewandte Chemie (International ed. in English) · 2025Article
- Strategies to Expand the Genetic Code of Mammalian Cells.Chemical reviews · 2025Review
- Optogenetics with Atomic Precision─A Comprehensive Review of Optical Control of Protein Function through Genetic Code Expansion.Chemical reviews · 2025Review
- Cracking the Code: Reprogramming the Genetic Script in Prokaryotes and Eukaryotes to Harness the Power of Noncanonical Amino Acids.Chemical reviews · 2024Review
- Directed Evolution of a Bacterial Leucyl tRNA in Mammalian Cells for Enhanced Noncanonical Amino Acid Mutagenesis.ACS synthetic biology · 2024Article
- Applications of genetic code expansion technology in eukaryotes.Protein & cell · 2024Review
- A Genetically Encoded Photocaged Cysteine for Facile Site-Specific Introduction of Conjugation-Ready Thiol Residues in Antibodies.Bioconjugate chemistry · 2024Article
- Article
- Biological and Catalytic Properties of Selenoproteins.International journal of molecular sciences · 2023Review
- Chemical synthesis of human selenoprotein F and elucidation of its thiol-disulfide oxidoreductase activity.Chemical science · 2022Article
- Non-canonical Amino Acid Substrates of E. coli Aminoacyl-tRNA Synthetases.Chembiochem : a European journal of chemical biology · 2022Review
- Expression of selenoproteins via genetic code expansion in mammalian cells.Methods in enzymology · 2022Article
- Article
- A FRET-ICT Dual-Modulated Ratiometric Fluorescence Sensor for Monitoring and Bio-Imaging of Cellular Selenocysteine.Molecules (Basel, Switzerland) · 2020Article
- Chemical Biology Approaches to Interrogate the Selenoproteome.Accounts of chemical research · 2019Review
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
Selenoproteins contain the amino acid selenocysteine (Sec) and are found in all domains of life. The functions of many selenoproteins are poorly understood, partly due to difficulties in producing recombinant selenoproteins for cell-biological evaluation. Endogenous mammalian selenoproteins are produced through a noncanonical translation mechanism requiring suppression of the UGA stop codon and a Sec insertion sequence (SECIS) element in the 3' untranslated region of the mRNA. Here, recombinant selenoproteins are generated in mammalian cells through genetic code expansion, circumventing the requirement for the SECIS element and selenium availability. An engineered orthogonal
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