ArticleMethods in enzymology2010
A highly purified, fluorescently labeled in vitro translation system for single-molecule studies of protein synthesis.
Article in Methods in enzymology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed.
- Multivalent weak contacts shape chaperone-nascent protein interactions.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Molecular mechanism of IF1- and IF2-driven translation initiation in bacteria.bioRxiv : the preprint server for biology · 2026Article
- A Microscale Platform for the Comprehensive Analysis of Bacterial Translation Initiation.International journal of molecular sciences · 2026Article
- Multivalent weak contacts shape chaperone-nascent protein interactions.bioRxiv : the preprint server for biology · 2026Article
- A cascade of structural rearrangements positions peptide release factor 2 for polypeptide hydrolysis on the ribosome.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- An RNA modification prevents extended codon-anticodon interactions from facilitating +1 frameshifting.Nature communications · 2025Article
- Time-domain event detection using single-instruction, multiple-thread gpGPU architectures in single-molecule biophysical data.Computer physics communications · 2024Article
- An easy tool to monitor the elemental steps of in vitro translation via gel electrophoresis of fluorescently labeled small peptides.RNA (New York, N.Y.) · 2024Article
- Entropic control of the free-energy landscape of an archetypal biomolecular machine.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Article
- Precise tuning of bacterial translation initiation by non-equilibrium 5'-UTR unfolding observed in single mRNAs.Nucleic acids research · 2022Article
- Site-Specific Fluorescent Labeling of RNA Interior Positions.Molecules (Basel, Switzerland) · 2021Review
- Insights into genome recoding from the mechanism of a classic +1-frameshifting tRNA.Nature communications · 2021Article
- Mechanistic studies of non-canonical amino acid mutagenesis.Methods in enzymology · 2021Article
- Article
- A Label-Free Assay for Aminoacylation of tRNA.Genes · 2020Article
- Multiplexed genomic encoding of non-canonical amino acids for labeling large complexes.Nature chemical biology · 2020Article
- The alarmones (p)ppGpp directly regulate translation initiation during entry into quiescence.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Article
- Coming Together: RNAs and Proteins Assemble under the Single-Molecule Fluorescence Microscope.Cold Spring Harbor perspectives in biology · 2019Review
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8 authors.
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Abstract
Single-molecule fluorescence resonance energy transfer (smFRET) has emerged as a powerful tool for mechanistic investigations of increasingly complex biochemical systems. Recently, we and others have successfully used smFRET to directly investigate the role of structural dynamics in the function and regulation of the cellular protein synthesis machinery. A significant challenge to these experiments, and to analogous experiments in similarly complex cellular machineries, is the need for specific and efficient fluorescent labeling of the biochemical system at locations that are both mechanistically informative and minimally perturbative to the biological activity. Here, we describe the development of a highly purified, fluorescently labeled in vitro translation system that we have successfully designed for smFRET studies of protein synthesis. The general approaches we outline should be amenable to single-molecule fluorescence studies of other complex biochemical systems.
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