ArticleJournal of the American Chemical Society2016
In Vivo Biosynthesis of a β-Amino Acid-Containing Protein.
Article in Journal of the American Chemical Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 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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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.
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Who cites it
78 citing papers in PubMed.
- Chemical Biology 2025: Highlights From the Ch/Bi145 Course at Caltech.Chembiochem : a European journal of chemical biology · 2026Review
- Co-Translational Incorporation ofJournal of the American Chemical Society · 2026Article
- Co-Translational Incorporation of (Journal of the American Chemical Society · 2026Article
- Site-selective protein editing by backbone extension acyl rearrangements.Nature chemical biology · 2025Article
- High throughput screening of eukaryotic release factor 1 variants to enhance noncanonical amino acid incorporation.bioRxiv : the preprint server for biology · 2025Article
- Monitoring monomer-specific acyl-tRNA levels in cells with PARTI.Nucleic acids research · 2025Article
- Biological Regulation StudiedAccounts of chemical research · 2025Article
- Expanding the genetic code: In vivo approaches for incorporating non-proteinogenic monomers.Journal of microbiology (Seoul, Korea) · 2025Review
- Peptide Backbone Editing via Post-Translational O to C Acyl Shift.Journal of the American Chemical Society · 2025Article
- RNA language models predict mutations that improve RNA function.Nature communications · 2024Article
- Metagenomic study of lake microbial mats reveals protease-inhibiting antiviral peptides from a core microbiome member.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Recent advances in the expanding genetic code.Current opinion in chemical biology · 2024Review
- Reaching New Heights in Genetic Code Manipulation with High Throughput Screening.Chemical reviews · 2024Review
- Engineering Pyrrolysine Systems for Genetic Code Expansion and Reprogramming.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
- RNA language models predict mutations that improve RNA function.bioRxiv : the preprint server for biology · 2024Article
- Application of artificial backbone connectivity in the development of metalloenzyme mimics.Current opinion in chemical biology · 2024Review
- β-Amino Acids Reduce Ternary Complex Stability and Alter the Translation Elongation Mechanism.ACS central science · 2024Article
- A Translation-Independent Directed Evolution Strategy to Engineer Aminoacyl-tRNA Synthetases.ACS central science · 2024Article
- Fine-tuning the tRNA anticodon arm for multiple/consecutive incorporations of β-amino acids and analogs.Nucleic acids research · 2024Article
18 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
5 authors.
Funding
Abstract
It has recently been reported that ribosomes from erythromycin-resistant Escherichia coli strains, when isolated in S30 extracts and incubated with chemically mis-acylated tRNA, can incorporate certain β-amino acids into full length DHFR in vitro. Here we report that wild-type E. coli EF-Tu and phenylalanyl-tRNA synthetase collaborate with these mutant ribosomes and others to incorporate β(3)-Phe analogs into full length DHFR in vivo. E. coli harboring the most active mutant ribosomes are robust, with a doubling time only 14% longer than wild-type. These results reveal the unexpected tolerance of E. coli and its translation machinery to the β(3)-amino acid backbone and should embolden in vivo selections for orthogonal translational machinery components that incorporate diverse β-amino acids into proteins and peptides. E. coli harboring mutant ribosomes may possess the capacity to incorporate many non-natural, non-α-amino acids into proteins and other sequence-programmed polymeric materials.
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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.