ArticleACS central science2024
β-Amino Acids Reduce Ternary Complex Stability and Alter the Translation Elongation Mechanism.
Article in ACS central science, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 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.
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.
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Who cites it
11 citing papers in PubMed.
- Enhancing ribosomal translation of backbone-altering nonproteinogenic amino acids via YebC and YeeN.Nucleic acids research · 2026Article
- Co-Translational Incorporation of (Journal of the American Chemical Society · 2026Article
- Co-Translational Incorporation ofJournal of the American Chemical Society · 2026Article
- Engineering of tRNAPro1E2 anticodon stem enhances multiple/consecutive ribosomal incorporation of N-methyl-l-α-amino acids and d-α-amino acids.Nucleic acids research · 2026Article
- Optimization of the genetic code expansion technology for intracellular labelling and single-molecule tracking of proteins in genomically re-codedRSC chemical biology · 2026Article
- Parallel stopped-flow interrogation of diverse biological systems at the single-molecule scale.Nature methods · 2026Article
- Site-selective protein editing by backbone extension acyl rearrangements.Nature chemical biology · 2025Article
- Direct and quantitative analysis of tRNA acylation using intact tRNA liquid chromatography-mass spectrometry.Nature protocols · 2025Review
- Monitoring monomer-specific acyl-tRNA levels in cells with PARTI.Nucleic acids research · 2025Article
- Thioesters Support Efficient Protein Biosynthesis by the Ribosome.ACS central science · 2025Article
- Incorporation of Multiple βACS central science · 2024Article
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Authors and funding
12 authors.
Funding
Abstract
Templated synthesis of proteins containing non-natural amino acids (nnAAs) promises to expand the chemical space available to biological therapeutics and materials, but existing technologies are still limiting. Addressing these limitations requires a deeper understanding of the mechanism of protein synthesis and how it is perturbed by nnAAs. Here we examine the impact of nnAAs on the formation and ribosome utilization of the central elongation substrate: the ternary complex of native, aminoacylated tRNA, thermally unstable elongation factor, and GTP. By performing ensemble and single-molecule fluorescence resonance energy transfer measurements, we reveal that both the (
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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 Socratic graph.