ArticleScience (New York, N.Y.)2011
Expanding the genetic code of Escherichia coli with phosphoserine.
Article in Science (New York, N.Y.), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 230 papers, 1 of them a synthesis that pooled it.
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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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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
230 citing papers in PubMed, 1 synthesis or guideline pooled it, 374 citations in OpenAlex.
- Cell-Free Approach for Non-canonical Amino Acids Incorporation Into Polypeptides.Frontiers in bioengineering and biotechnology · 2020Pooled it
- Ribosome engineering enhances genetic code expansion inSynthetic and systems biotechnology · 2027Article
- Automated prototyping of genetic codes.Nature · 2026Article
- GSK3β and Plk1 sequentially phosphorylate ATP-citrate lyase to promote homologous recombination.Science advances · 2026Article
- Cold Orthogonal Translation: A Psychrophilic Pyrrolysyl-tRNA Synthetase Boosts Genetic Code Expansion in E. coli.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Genetic Code Expansion, Enzymatic Modification, and C-Terminal Labeling Enable Facile Production of Highly Modified α-Synuclein.bioRxiv : the preprint server for biology · 2026Article
- Cryo-EM structure of the LARS1:IARS1 complex reveals a nutrient-responsive switch controlling mTORC1 signaling.Nature communications · 2026Article
- Mechanistic insights on spatiotemporal control of Ras-signaling.Biological chemistry · 2026Review
- Selecting aminoacyl-tRNA synthetase/tRNA pairs for efficient genetic encoding of noncanonical amino acids into proteins.Nature protocols · 2026Review
- STARD3 regulates lysosome positioning and contacts via a GSK3-controlled phosphorylation switch.The EMBO journal · 2026Article
- Accessing intractable, phosphorylated intrinsically disordered proteins via a protease-cleavable inclusion body tag.Protein science : a publication of the Protein Society · 2026Article
- Recoding multiple rare codons enables the simultaneous incorporation of up to five distinct noncanonical amino acids.Nature chemistry · 2026Article
- Methods for studying the effects of phosphorylation patterns in proteins.Biochemical Society transactions · 2026Review
- Sensitive detection of cancer antigens enabled by user-defined peptide libraries.Nature biotechnology · 2026Article
- High throughput screening of eukaryotic release factor 1 variants to enhance noncanonical amino acid incorporation.bioRxiv : the preprint server for biology · 2025Article
- The cAMP-PKA signaling initiates mitosis by phosphorylating Bora.Nature communications · 2025Article
- A Tailored Phospho-p53 Library Probes Antibody Specificity and Recognition Limitations.Chembiochem : a European journal of chemical biology · 2025Article
- Scientific and technological challenges of recombinant egg protein production.BMC biotechnology · 2025Review
- Efficient genetic code expansion without host genome modifications.Nature biotechnology · 2025Article
- Directed evolution of aminoacyl-tRNA synthetases through in vivo hypermutation.Nature communications · 2025Article
170 more citing papers are in PubMed but not listed here.
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
O-Phosphoserine (Sep), the most abundant phosphoamino acid in the eukaryotic phosphoproteome, is not encoded in the genetic code, but synthesized posttranslationally. Here, we present an engineered system for specific cotranslational Sep incorporation (directed by UAG) into any desired position in a protein by an Escherichia coli strain that harbors a Sep-accepting transfer RNA (tRNA(Sep)), its cognate Sep-tRNA synthetase (SepRS), and an engineered EF-Tu (EF-Sep). Expanding the genetic code rested on reengineering EF-Tu to relax its quality-control function and permit Sep-tRNA(Sep) binding. To test our system, we synthesized the activated form of human mitogen-activated ERK activating kinase 1 (MEK1) with either one or two Sep residues cotranslationally inserted in their canonical positions (Sep(218), Sep(222)). This system has general utility in protein engineering, molecular biology, and disease research.
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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.