ArticleNature communications2022
Ribosome-mediated biosynthesis of pyridazinone oligomers in vitro.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Co-Translational Incorporation of (Journal of the American Chemical Society · 2026Article
- Chemical and ribosomal synthesis of atropisomeric and macrocyclic peptides with embedded quinolines.Nature chemistry · 2026Article
- Expanded ribosomal synthesis of non-standard cyclic backbones in vitro.Nature communications · 2025Article
- Direct and quantitative analysis of tRNA acylation using intact tRNA liquid chromatography-mass spectrometry.Nature protocols · 2025Review
- Cell-free protein synthesis platforms for accelerating drug discovery.Biotechnology notes (Amsterdam, Netherlands) · 2025Review
- Cell-Free Systems: Ideal Platforms for Accelerating the Discovery and Production of Peptide-Based Antibiotics.International journal of molecular sciences · 2024Review
- A Translation-Independent Directed Evolution Strategy to Engineer Aminoacyl-tRNA Synthetases.ACS central science · 2024Article
- Engineering tRNAs for the Ribosomal Translation of Non-proteinogenic Monomers.Chemical reviews · 2024Review
- Tuning tRNAs for improved translation.Frontiers in genetics · 2024Review
- Expanding the substrate scope of pyrrolysyl-transfer RNA synthetase enzymes to include non-α-amino acids in vitro and in vivo.Nature chemistry · 2023Article
- Aminobenzoic Acid Derivatives Obstruct Induced Fit in the Catalytic Center of the Ribosome.ACS central science · 2023Article
Corrections and comments
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Authors and funding
12 authors.
Funding
Abstract
The ribosome is a macromolecular machine that catalyzes the sequence-defined polymerization of L-α-amino acids into polypeptides. The catalysis of peptide bond formation between amino acid substrates is based on entropy trapping, wherein the adjacency of transfer RNA (tRNA)-coupled acyl bonds in the P-site and the α-amino groups in the A-site aligns the substrates for coupling. The plasticity of this catalytic mechanism has been observed in both remnants of the evolution of the genetic code and modern efforts to reprogram the genetic code (e.g., ribosomal incorporation of non-canonical amino acids, ribosomal ester formation). However, the limits of ribosome-mediated polymerization are underexplored. Here, rather than peptide bonds, we demonstrate ribosome-mediated polymerization of pyridazinone bonds via a cyclocondensation reaction between activated γ-keto and α-hydrazino ester monomers. In addition, we demonstrate the ribosome-catalyzed synthesis of peptide-hybrid oligomers composed of multiple sequence-defined alternating pyridazinone linkages. Our results highlight the plasticity of the ribosome's ancient bond-formation mechanism, expand the range of non-canonical polymeric backbones that can be synthesized by the ribosome, and open the door to new applications in synthetic biology.
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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 Socratic graph.