ArticleNature communications2018
Cell-free protein synthesis from genomically recoded bacteria enables multisite incorporation of noncanonical amino acids.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 105 papers, 1 of them a synthesis that pooled it.
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Who cites it
105 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Cell-Free Approach for Non-canonical Amino Acids Incorporation Into Polypeptides.Frontiers in bioengineering and biotechnology · 2020Pooled it
- Selective elimination of mast cells via Siglec-6-targeted nanodelivery of drug payload.The Journal of allergy and clinical immunology · 2026Article
- Article
- Is faster always better? A critical assessment of Vibrio natriegens as microbial host for recombinant protein production.Bioprocess and biosystems engineering · 2026Review
- Microbial cell-free protein synthesis and its progression toward industrial use.Microbiology (Reading, England) · 2026Review
- Genomically integrated orthogonal translation system in Escherichia coli enables production of functional modified [NiFe]-hydrogenases.Microbial cell factories · 2026Article
- Artificial initiation codons and engineered initiator tRNAs enable N-terminal noncanonical amino acid incorporation in intact cell-free translation systems.bioRxiv : the preprint server for biology · 2026Article
- Design-driven optimization of low-cost reagent formulations for reproducible and high-yielding cell-free gene expression.Nature communications · 2026Article
- Purification of post-transcriptionally modified tRNAs for enhanced cell-free translation systems.Nucleic acids research · 2026Article
- A Simple and Versatile Cell-Free Expression Method for Producing Secondary Metabolites.ACS synthetic biology · 2026Article
- Characterizing Cell-Free Transcription and Translation Dynamics with Nucleic Acid-Based Assays.ACS synthetic biology · 2026Article
- Marine-Inspired Antimicrobial Peptides Disrupt Gene Expression at the DNA Level.ACS infectious diseases · 2026Article
- Harnessing Plasmid Crosstalk in Transcription Factor Mediated Cell-Free Biosensors.bioRxiv : the preprint server for biology · 2025Article
- Engineered orthogonal translation systems from metagenomic libraries expand the genetic code.bioRxiv : the preprint server for biology · 2025Article
- Automated and Programmable Cell-Free Systems for Scalable Synthetic Biology with a Focus on Biofoundry Integration.Journal of microbiology and biotechnology · 2025Review
- Online monitoring of the mitochondrial respiration activity and protein formation in the Almost Living Cell-free Expression (ALiCE) system.BMC biotechnology · 2025Article
- Cell-free protein synthesis and vesicle systems for programmable therapeutic manufacturing and delivery.Journal of biological engineering · 2025Review
- BeyondChemical reviews · 2025Review
- Cell-Free Gene Expression: Methods and Applications.Chemical reviews · 2025Review
- Defining serine tRNA knockout as a strategy for effective repression of gene expression in organisms with a recoded genome.Nucleic acids research · 2025Article
45 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
18 authors.
Funding
Abstract
Cell-free protein synthesis has emerged as a powerful approach for expanding the range of genetically encoded chemistry into proteins. Unfortunately, efforts to site-specifically incorporate multiple non-canonical amino acids into proteins using crude extract-based cell-free systems have been limited by release factor 1 competition. Here we address this limitation by establishing a bacterial cell-free protein synthesis platform based on genomically recoded Escherichia coli lacking release factor 1. This platform was developed by exploiting multiplex genome engineering to enhance extract performance by functionally inactivating negative effectors. Our most productive cell extracts enabled synthesis of 1,780 ± 30 mg/L superfolder green fluorescent protein. Using an optimized platform, we demonstrated the ability to introduce 40 identical p-acetyl-L-phenylalanine residues site specifically into an elastin-like polypeptide with high accuracy of incorporation ( ≥ 98%) and yield (96 ± 3 mg/L). We expect this cell-free platform to facilitate fundamental understanding and enable manufacturing paradigms for proteins with new and diverse chemistries.
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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.