ArticlePloS one2014
Synthesis of non-linear protein dimers through a genetically encoded Thiol-ene reaction.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed.
- Hydrochalcogenation Reactions with Noncanonical Amino Acids as a Route to Increase Bioconjugate Valency.ACS omega · 2025Article
- Engineering Pyrrolysine Systems for Genetic Code Expansion and Reprogramming.Chemical reviews · 2024Review
- Designed Artificial Protein Heterodimers With Coupled Functions Constructed Using Bio-Orthogonal Chemistry.Frontiers in chemistry · 2021Article
- Genetic code expansion in mammalian cells: A plasmid system comparison.Bioorganic & medicinal chemistry · 2020Article
- In-Cell Synthesis of Bioorthogonal Alkene Tag S-Allyl-Homocysteine and Its Coupling with Reprogrammed Translation.International journal of molecular sciences · 2019Article
- The First MS-Cleavable, Photo-Thiol-Reactive Cross-Linker for Protein Structural Studies.Journal of the American Society for Mass Spectrometry · 2019Article
- Genetic Code Expansion in Animals.ACS chemical biology · 2018Review
- Incorporation of Amino Acids with Long-Chain Terminal Olefins into Proteins.Molecules (Basel, Switzerland) · 2016Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Site-specific incorporation of bioorthogonal unnatural amino acids into proteins provides a useful tool for the installation of specific functionalities that will allow for the labeling of proteins with virtually any probe. We demonstrate the genetic encoding of a set of alkene lysines using the orthogonal PylRS/PylTCUA pair in Escherichia coli. The installed double bond functionality was then applied in a photoinitiated thiol-ene reaction of the protein with a fluorescent thiol-bearing probe, as well as a cysteine residue of a second protein, showing the applicability of this approach in the formation of heterogeneous non-linear fused proteins.
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Registered trials
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