ReviewChemical science2015
Designing logical codon reassignment - Expanding the chemistry in biology.
Review in Chemical science, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 254 papers, 1 of them a synthesis that pooled it.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
254 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Cell-Free Approach for Non-canonical Amino Acids Incorporation Into Polypeptides.Frontiers in bioengineering and biotechnology · 2020Pooled it
- Genetic code expansion enables plant-directed control of bacterial activity.Nature biotechnology · 2026Article
- Site-Specific Protein Bioconjugation Through Cellular Incorporation of Noncanonical Amino Acids.Angewandte Chemie (International ed. in English) · 2026Review
- Article
- Directed Evolution of Threonine Aldolases for the Photobiocatalytic Synthesis of β-Branched-α-Tetrasubstituted and Other Noncanonical Amino Acids.Journal of the American Chemical Society · 2026Article
- Combined biosynthesis and site-specific incorporation of phenylalanine derivatives from aryl aldehydes or carboxylic acids.Nature communications · 2026Article
- Unraveling Synthetase's Mode of Action: The Pyrrolysyl-tRNA Synthetase Dimer Uses Secondary Binding Sites in the Cell.Angewandte Chemie (International ed. in English) · 2026Article
- Site-Specific Antigen Immobilization Improves Autoantibody Binding Efficiency on the Luminex Platform.ACS omega · 2026Article
- Selecting aminoacyl-tRNA synthetase/tRNA pairs for efficient genetic encoding of noncanonical amino acids into proteins.Nature protocols · 2026Review
- Recoding multiple rare codons enables the simultaneous incorporation of up to five distinct noncanonical amino acids.Nature chemistry · 2026Article
- Nonheme Fe Enzyme-Catalyzed Enantiodivergent Nitrogen Migration: Directed Evolution and Computational Study of Isopenicillin N Synthases for Biocatalytic Synthesis of Arylglycines.Angewandte Chemie (International ed. in English) · 2026Article
- Cell-selective multiplexed bioorthogonal noncanonical amino acid tagging for nascent proteomics.Nature chemical biology · 2026Article
- Genetic Encoding of Pentafluorophosphato-Phenylalanine Provides PFAngewandte Chemie (International ed. in English) · 2026Article
- Article
- Biocompatible Chemistry: A Plug-and-Play Toolbox for Chemical Biology Research.Chembiochem : a European journal of chemical biology · 2025Review
- Nonheme Fe 1,3-nitrogen migratases for asymmetric noncanonical amino acid synthesis.Nature chemical biology · 2025Article
- Engineered orthogonal translation systems from metagenomic libraries expand the genetic code.bioRxiv : the preprint server for biology · 2025Article
- Stereoselective diversification of α-amino acids enabled by N-heterocyclic carbene catalysis.Nature communications · 2025Article
- Genetic code expansion and enzymatic modifications as accessible methods for studying site-specific post-translational modifications of alpha-synuclein and tau.Protein science : a publication of the Protein Society · 2025Article
- A robust platform streamlining aromatic noncanonical amino acid biosynthesis and genetic code expansion in Escherichia coli.Nature communications · 2025Article
194 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
Abstract
Over the last decade, the ability to genetically encode unnatural amino acids (UAAs) has evolved rapidly. The programmed incorporation of UAAs into recombinant proteins relies on the reassignment or suppression of canonical codons with an amino-acyl tRNA synthetase/tRNA (aaRS/tRNA) pair, selective for the UAA of choice. In order to achieve selective incorporation, the aaRS should be selective for the designed tRNA and UAA over the endogenous amino acids and tRNAs. Enhanced selectivity has been achieved by transferring an aaRS/tRNA pair from another kingdom to the organism of interest, and subsequent aaRS evolution to acquire enhanced selectivity for the desired UAA. Today, over 150 non-canonical amino acids have been incorporated using such methods. This enables the introduction of a large variety of structures into proteins, in organisms ranging from prokaryote, yeast and mammalian cells lines to whole animals, enabling the study of protein function at a level that could not previously be achieved. While most research to date has focused on the suppression of 'non-sense' codons, recent developments are beginning to open up the possibility of quadruplet codon decoding and the more selective reassignment of sense codons, offering a potentially powerful tool for incorporating multiple amino acids. Here, we aim to provide a focused review of methods for UAA incorporation with an emphasis in particular on the different tRNA synthetase/tRNA pairs exploited or developed, focusing upon the different UAA structures that have been incorporated and the logic behind the design and future creation of such systems. Our hope is that this will help rationalize the design of systems for incorporation of unexplored unnatural amino acids, as well as novel applications for those already known.
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.