ArticleNucleic acids research2012
Real-time assay for testing components of protein synthesis.
Article in Nucleic acids research, 2012. 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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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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Who cites it
11 citing papers in PubMed, 20 citations in OpenAlex.
- FAST, a method based on split-GFP for the detection in solution of proteins synthesized in cell-free expression systems.Scientific reports · 2024Article
- Continuous Fluorescence Assay for In Vitro Translation Compatible with Noncanonical Amino Acids.ACS synthetic biology · 2024Article
- Cytosolic GDH1 degradation restricts protein synthesis to sustain tumor cell survival following amino acid deprivation.The EMBO journal · 2021Article
- A Novel Method to Evaluate Ribosomal Performance in Cell-Free Protein Synthesis Systems.Scientific reports · 2017Article
- A High-Throughput Screening Assay Using a Photoconvertable Protein for Identifying Inhibitors of Transcription, Translation, or Proteasomal Degradation.SLAS discovery : advancing life sciences R & D · 2017Article
- Ribosome-Templated Azide-Alkyne Cycloadditions: Synthesis of Potent Macrolide Antibiotics by In Situ Click Chemistry.Journal of the American Chemical Society · 2016Article
- EF-Tu dynamics during pre-translocation complex formation: EF-Tu·GDP exits the ribosome via two different pathways.Nucleic acids research · 2015Article
- A simple real-time assay for in vitro translation.RNA (New York, N.Y.) · 2015Article
- Engine out of the chassis: cell-free protein synthesis and its uses.FEBS letters · 2014Review
- Quantifying elongation rhythm during full-length protein synthesis.Journal of the American Chemical Society · 2013Article
- Tb(3+)-tRNA for LRET studies of protein synthesis.Bioconjugate chemistry · 2013Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
We present a flexible, real-time-coupled transcription-translation assay that involves the continuous monitoring of fluorescent Emerald GFP formation. Along with numerical simulation of a reaction kinetics model, the assay permits quantitative estimation of the effects on full-length protein synthesis of various additions, subtractions or substitutions to the protein synthesis machinery. Since the assay uses continuous fluorescence monitoring, it is much simpler and more rapid than other assays of protein synthesis and is compatible with high-throughput formats. Straightforward alterations of the assay permit determination of (i) the fraction of ribosomes in a cell-free protein synthesis kit that is active in full-length protein synthesis and (ii) the relative activities in supporting protein synthesis of modified (e.g. mutated, fluorescent-labeled) exogenous components (ribosomes, amino acid-specific tRNAs) that replace the corresponding endogenous components. Ribosomes containing fluorescent-labeled L11 and tRNAs labeled with fluorophores in the D-loop retain substantial activity. In the latter case, the extent of activity loss correlates with a combination of steric bulk and hydrophobicity of the fluorophore.
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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.