ArticleBiotechnology journal2022
An efficient cell-free protein synthesis platform for producing proteins with pyrrolysine-based noncanonical amino acids.
Article in Biotechnology journal, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 14 citations in OpenAlex.
- Noncanonical amino acids enable plug and play vaccine platform in the ALiCE cell free system.NPJ vaccines · 2026Article
- Reaching New Heights in Genetic Code Manipulation with High Throughput Screening.Chemical reviews · 2024Review
- Engineering Pyrrolysine Systems for Genetic Code Expansion and Reprogramming.Chemical reviews · 2024Review
- Crystal Structure of Pyrrolysyl-tRNA Synthetase from a Methanogenic Archaeon ISO4-G1 and Its Structure-Based Engineering for Highly-Productive Cell-Free Genetic Code Expansion with Non-Canonical Amino Acids.International journal of molecular sciences · 2023Article
- Enabling Genetic Code Expansion and Peptide Macrocyclization in mRNA Display via a Promiscuous Orthogonal Aminoacyl-tRNA Synthetase.Journal of the American Chemical Society · 2023Article
- Bottom-Up Synthetic Biology Using Cell-Free Protein Synthesis.Advances in biochemical engineering/biotechnology · 2023Review
- Advancing synthetic biology through cell-free protein synthesis.Computational and structural biotechnology journal · 2023Review
- Utilizing a cell-free protein synthesis platform for the biosynthesis of a natural product, caffeine.Synthetic biology (Oxford, England) · 2023Article
- A ubiquitous amino acid source for prokaryotic and eukaryotic cell-free transcription-translation systems.Frontiers in bioengineering and biotechnology · 2022Article
- Delivery of the selenoprotein thioredoxin reductase 1 to mammalian cells.Frontiers in molecular biosciences · 2022Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Incorporation of noncanonical amino acids (ncAAs) into proteins opens new opportunities in biotechnology and synthetic biology. Pyrrolysine (Pyl)-based ncAAs are some of the most predominantly used, but expression systems suffer from low yields. Here, we report a highly efficient cell-free protein synthesis (CFPS) platform for site-specific incorporation of Pyl-based ncAAs into proteins using amber suppression. This platform is based on cellular extracts derived from genomically recoded Escherichia coli lacking release factor 1 and enhanced through deletion of endonuclease A. To enable ncAA incorporation, orthogonal translation system (OTS) components (i.e., the orthogonal transfer RNA [tRNA] and orthogonal aminoacyl tRNA synthetase) were coexpressed in the source strain prior to lysis and the orthogonal tRNA
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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.