ArticleNature chemistry2014
Optimized orthogonal translation of unnatural amino acids enables spontaneous protein double-labelling and FRET.
Article in Nature chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 140 papers.
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.
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Who cites it
140 citing papers in PubMed, 269 citations in OpenAlex.
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- Genetic Code Expansion for Site-Specific Encoding of a Switchable, Intrinsic Fluorophore-Quencher Pair to Monitor Protein Dynamics.bioRxiv : the preprint server for biology · 2026Article
- Tools For Building Artificial Biological Nanostructures.ACS nano · 2026Review
- Development and Optimization of an Aminooxy Coupling Reaction to Prepare Multivalent Bioconjugates with a Single Noncanonical Amino Acid.Bioconjugate chemistry · 2026Article
- Correlating membrane-protein dynamics with function: Integrating bioinformatics, molecular dynamics, and single-molecule FRET.Protein science : a publication of the Protein Society · 2025Article
- Tuning Encodable Tetrazine Chemistry for Site-Specific Protein Bioorthogonal Ligations.Angewandte Chemie (International ed. in English) · 2025Article
- Cyanophenylalanine as an Infrared Probe for Iron-Sulfur Cluster Redox State in Multicenter Metalloenzymes.Chembiochem : a European journal of chemical biology · 2025Article
- Efficient genetic code expansion without host genome modifications.Nature biotechnology · 2025Article
- Monitoring SARS-CoV-2 Nsp13 helicase binding activity using expanded genetic code techniques.RSC chemical biology · 2025Article
- Strategies to Expand the Genetic Code of Mammalian Cells.Chemical reviews · 2025Review
- Genetic Code Expansion: Recent Developments and Emerging Applications.Chemical reviews · 2025Review
- Genetic Code Expansion Approaches to Decipher the Ubiquitin Code.Chemical reviews · 2024Review
- Directed Evolution ofACS bio & med chem Au · 2024Article
- Engineering Pyrrolysine Systems for Genetic Code Expansion and Reprogramming.Chemical reviews · 2024Review
- Cellular Site-Specific Incorporation of Noncanonical Amino Acids in Synthetic Biology.Chemical reviews · 2024Review
- Cracking the Code: Reprogramming the Genetic Script in Prokaryotes and Eukaryotes to Harness the Power of Noncanonical Amino Acids.Chemical reviews · 2024Review
- Genetic Code Expansion inACS synthetic biology · 2024Article
- Directed Evolution of a Bacterial Leucyl tRNA in Mammalian Cells for Enhanced Noncanonical Amino Acid Mutagenesis.ACS synthetic biology · 2024Article
- Mutually Orthogonal Bioorthogonal Reactions: Selective Chemistries for Labeling Multiple Biomolecules Simultaneously.Topics in current chemistry (Cham) · 2024Review
80 more citing papers are in PubMed but not listed here.
Corrections and comments
- Commented on by
- Erratum issuedWilf, Nabil W [corrected to Wilf, Nabil M]
Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
The ability to introduce different biophysical probes into defined positions in target proteins will provide powerful approaches for interrogating protein structure, function and dynamics. However, methods for site-specifically incorporating multiple distinct unnatural amino acids are hampered by their low efficiency. Here we provide a general solution to this challenge by developing an optimized orthogonal translation system that uses amber and evolved quadruplet-decoding transfer RNAs to encode numerous pairs of distinct unnatural amino acids into a single protein expressed in Escherichia coli with a substantial increase in efficiency over previous methods. We also provide a general strategy for labelling pairs of encoded unnatural amino acids with different probes via rapid and spontaneous reactions under physiological conditions. We demonstrate the utility of our approach by genetically directing the labelling of several pairs of sites in calmodulin with fluorophores and probing protein structure and dynamics by Förster resonance energy transfer.
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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.