ArticleACS synthetic biology2023
Regulated N-Terminal Modification of Proteins Synthesized Using a Reconstituted Cell-Free Protein Synthesis System.
Article in ACS synthetic biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed.
- MAXTIA: A high-throughput platform for rapid functional epitope mapping by kinetic screening of mutant libraries.Protein science : a publication of the Protein Society · 2026Article
- Mechanistic insights on spatiotemporal control of Ras-signaling.Biological chemistry · 2026Review
- N-terminal modifications as fate switches in neurodegeneration: a mechanistic review.Frontiers in aging neuroscience · 2026Review
- On-demand insulin manufacturing using cell-free systems with an "on-column" conversion approach.New biotechnology · 2025Article
- Lipid Modification and Membrane Localization of Proteins in Cell-Free System.ACS synthetic biology · 2025Article
- Structural insights into lab-coevolved RNA-RBP pairs and applications of synthetic riboswitches in cell-free system.Nucleic acids research · 2025Article
- N-Terminal Amino Acid Affects the Translation Efficiency at Lower Temperatures in a Reconstituted Protein Synthesis System.International journal of molecular sciences · 2024Article
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6 authors.
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Abstract
The N-terminal modification of nascent proteins, such as acetylation and myristoylation, is one of the most abundant post-translational modifications. To analyze the function of the modification, it is important to compare the modified and unmodified proteins under defined conditions. However, it is technically difficult to prepare unmodified proteins because cell-based systems contain endogenous modification systems. In this study, we developed a cell-free method to conduct N-terminal acetylation and myristoylation of nascent proteins
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