ArticleProceedings of the National Academy of Sciences of the United States of America2006
Enzymatic aminoacylation of tRNA with unnatural amino acids.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers, 1 of them a synthesis that pooled it.
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Who cites it
54 citing papers in PubMed, 1 synthesis or guideline pooled it, 150 citations in OpenAlex.
- Cell-Free Approach for Non-canonical Amino Acids Incorporation Into Polypeptides.Frontiers in bioengineering and biotechnology · 2020Pooled it
- Systematic Profiling of Peptide Substrate Specificity in N-Terminal Processing by Methionine Aminopeptidase Using mRNA Display and an Unnatural Methionine Analogue.ACS chemical biology · 2026Article
- Article
- Direct and quantitative analysis of tRNA acylation using intact tRNA liquid chromatography-mass spectrometry.Nature protocols · 2025Review
- Breaking the Degeneracy of Sense Codons - How Far Can We Go?Israel journal of chemistry · 2024Article
- Evolution of Pyrrolysyl-tRNA Synthetase: From Methanogenesis to Genetic Code Expansion.Chemical reviews · 2024Review
- Continuous Fluorescence Assay for In Vitro Translation Compatible with Noncanonical Amino Acids.ACS synthetic biology · 2024Article
- Sequence-based prediction of the intrinsic solubility of peptides containing non-natural amino acids.Nature communications · 2023Article
- Non-Canonical Amino Acids in Analyses of Protease Structure and Function.International journal of molecular sciences · 2023Review
- Extensive breaking of genetic code degeneracy with non-canonical amino acids.Nature communications · 2023Article
- THRONCAT: metabolic labeling of newly synthesized proteins using a bioorthogonal threonine analog.Nature communications · 2023Article
- p-Chloropropynyl Phenylalanine, a Versatile Non-Canonical Amino Acid for Co-Translational Peptide Macrocyclization and Side Chain Diversification.Chembiochem : a European journal of chemical biology · 2023Article
- Development of a Cyclic, Cell Penetrating Peptide Compatible with In Vitro Selection Strategies.ACS chemical biology · 2023Article
- Expansion of the genetic code through reassignment of redundant sense codons using fully modified tRNA.Nucleic acids research · 2022Article
- Active site remodelling of a cyclodipeptide synthase redefines substrate scope.Communications chemistry · 2022Article
- Non-canonical Amino Acid Substrates of E. coli Aminoacyl-tRNA Synthetases.Chembiochem : a European journal of chemical biology · 2022Review
- Biochemistry of Aminoacyl tRNA Synthetase and tRNAs and Their Engineering for Cell-Free and Synthetic Cell Applications.Frontiers in bioengineering and biotechnology · 2022Review
- Nature-Inspired Circular-Economy Recycling for Proteins: Proof of Concept.Advanced materials (Deerfield Beach, Fla.) · 2021Article
- Directing evolution of novel ligands by mRNA display.Chemical Society reviews · 2021Review
- Is Exposure to BMAA a Risk Factor for Neurodegenerative Diseases? A Response to a Critical Review of the BMAA Hypothesis.Neurotoxicity research · 2021Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The biochemical flexibility of the cellular translation apparatus offers, in principle, a simple route to the synthesis of drug-like modified peptides and novel biopolymers. However, only approximately 75 unnatural building blocks are known to be fully compatible with enzymatic tRNA acylation and subsequent ribosomal synthesis of modified peptides. Although the translation system can reject substrate analogs at several steps along the pathway to peptide synthesis, much of the specificity resides at the level of the aminoacyl-tRNA synthetase (AARS) enzymes that are responsible for charging tRNAs with amino acids. We have developed an AARS assay based on mass spectrometry that can be used to rapidly identify unnatural monomers that can be enzymatically charged onto tRNA. By using this assay, we have found 59 previously unknown AARS substrates. These include numerous side-chain analogs with useful functional properties. Remarkably, many beta-amino acids, N-methyl amino acids, and alpha,alpha-disubstituted amino acids are also AARS substrates. These previously unidentified AARS substrates will be useful in studies of the specificity of subsequent steps in translation and may significantly expand the number of analogs that can be used for the ribosomal synthesis of modified peptides.
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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.