ArticleJournal of molecular biology2020
Overcoming Near-Cognate Suppression in a Release Factor 1-Deficient Host with an Improved Nitro-Tyrosine tRNA Synthetase.
Article in Journal of molecular biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
- Genetic Encoding of 3-Cyano-Tyrosine and Its Use in Controlling the Chromophore Isomeric State of the Fluorescent Protein mKate.International journal of molecular sciences · 2026Article
- Efficient and Site-Specific Incorporation of 3-Nitro-Tyrosine Into Recombinant Proteins inBio-protocol · 2026Article
- Selecting aminoacyl-tRNA synthetase/tRNA pairs for efficient genetic encoding of noncanonical amino acids into proteins.Nature protocols · 2026Review
- Engineered orthogonal translation systems from metagenomic libraries expand the genetic code.bioRxiv : the preprint server for biology · 2025Article
- Tuning Encodable Tetrazine Chemistry for Site-Specific Protein Bioorthogonal Ligations.Angewandte Chemie (International ed. in English) · 2025Article
- Nitration-driven structural changes in Hsp90 linked to gain of pathological functions.The Biochemical journal · 2025Article
- Quantitative Protein Labeling in Live Cells by Controlling the Redox State of Encoded Tetrazines.Journal of the American Chemical Society · 2025Article
- Unraveling the molecular basis of substrate specificity and halogen activation in vanadium-dependent haloperoxidases.Nature communications · 2025Article
- Artificial Intelligence Transforming Post-Translational Modification Research.Bioengineering (Basel, Switzerland) · 2024Review
- Genetic Encoding of Phosphorylated Amino Acids into Proteins.Chemical reviews · 2024Review
- Orthogonal Translation for Site-Specific Installation of Post-translational Modifications.Chemical reviews · 2024Review
- Truncation-Free Genetic Code Expansion with Tetrazine Amino Acids for Quantitative Protein Ligations.Bioconjugate chemistry · 2023Article
- Ultrafast Bioorthogonal Spin-Labeling and Distance Measurements in Mammalian Cells Using Small, Genetically Encoded Tetrazine Amino Acids.Journal of the American Chemical Society · 2023Article
- Autonomous Synthesis of Functional, Permanently Phosphorylated Proteins for Defining the Interactome of Monomeric 14-3-3ζ.ACS central science · 2023Article
- Site-specific dual encoding and labeling of proteins via genetic code expansion.Cell chemical biology · 2023Review
- Functional analysis of protein post-translational modifications using genetic codon expansion.Protein science : a publication of the Protein Society · 2023Review
- High-yield recombinant bacterial expression ofProtein science : a publication of the Protein Society · 2023Article
- Ultra-Fast Bioorthogonal Spin-Labeling and Distance Measurements in Mammalian Cells Using Small, Genetically Encoded Tetrazine Amino Acids.bioRxiv : the preprint server for biology · 2023Article
- Generating EfficientACS chemical biology · 2022Article
- Accessing isotopically labeled proteins containing genetically encoded phosphoserine for NMR with optimized expression conditions.The Journal of biological chemistry · 2022Article
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
Genetic code expansion (GCE) technologies incorporate non-canonical amino acids (ncAAs) into proteins at amber stop codons. To avoid unwanted truncated protein and improve ncAA-protein yields, genomically recoded strains of Escherichia coli lacking Release Factor 1 (RF1) are becoming increasingly popular expression hosts for GCE applications. In the absence of RF1, however, endogenous near-cognate amber suppressing tRNAs can lead to contaminating protein forms with natural amino acids in place of the ncAA. Here, we show that a second-generation amino-acyl tRNA synthetase (aaRS)/tRNA
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