ArticleNature protocols2011
Multifunctional protein labeling via enzymatic N-terminal tagging and elaboration by click chemistry.
Article in Nature protocols, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 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
56 citing papers in PubMed.
- Advancements and applications of click chemistry in protein labeling and bioconjugation.RSC advances · 2026Review
- Monitoring host-pathogen interactions using chemical proteomics.RSC chemical biology · 2024Review
- Immobilization of azide-functionalized proteins to micro- and nanoparticles directly from cell lysate.Mikrochimica acta · 2023Article
- Analysis of CDPK1 targets identifies a trafficking adaptor complex that regulates microneme exocytosis ineLife · 2023Article
- Promiscuous Enzymes for Residue-Specific Peptide and Protein Late-Stage Functionalization.Chembiochem : a European journal of chemical biology · 2023Review
- Analysis of CDPK1 targets identifies a trafficking adaptor complex that regulates microneme exocytosis inbioRxiv : the preprint server for biology · 2023Article
- Monitoring cell membrane recycling dynamics of proteins using whole-cell fluorescence recovery after photobleaching of pH-sensitive genetic tags.Nature protocols · 2022Review
- PAL-Mediated Ligation for Protein and Cell-Surface Modification.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Review
- The Art of Engineering Biomimetic Cellular Microenvironments.ACS biomaterials science & engineering · 2021Article
- A Not-So-Ancient Grease History: Click Chemistry and Protein Lipid Modifications.Chemical reviews · 2021Review
- Exploiting Protein N-Terminus for Site-Specific Bioconjugation.Molecules (Basel, Switzerland) · 2021Review
- Regulatory effects of protein S-acylation on insulin secretion and insulin action.Open biology · 2021Review
- Novel Thienopyrimidine Inhibitors ofJournal of medicinal chemistry · 2020Article
- Profiling of myristoylation ineLife · 2020Article
- Acylation-coupled lipophilic induction of polarisation (Acyl-cLIP): a universal assay for lipid transferase and hydrolase enzymes.Chemical science · 2019Article
- Genetically Encoded Photocleavable Linkers for Patterned Protein Release from Biomaterials.Journal of the American Chemical Society · 2019Article
- Analysis of a fully infectious bio-orthogonally modified human virus reveals novel features of virus cell entry.PLoS pathogens · 2019Article
- Concurrent Delivery of Soluble and Immobilized Proteins to Recruit and Differentiate Neural Stem Cells.Biomacromolecules · 2019Article
- Structure-Guided Identification of Resistance Breaking Antimalarial N‑Myristoyltransferase Inhibitors.Cell chemical biology · 2019Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
A protocol for selective and site-specific enzymatic labeling of proteins is described. The method exploits the protein co-/post-translational modification known as myristoylation, the transfer of myristic acid (a 14-carbon saturated fatty acid) to an N-terminal glycine catalyzed by the enzyme myristoyl-CoA:protein N-myristoyltransferase (NMT). Escherichia coli, having no endogenous NMT, is used for the coexpression of both the transferase and the target protein to be labeled, which participate in the in vivo N-terminal attachment of synthetically derived tagged analogs of myristic acid bearing a 'clickable' tag. This tag is a functional group that can undergo bio-orthogonal ligation via 'click' chemistry, for example, an azide, and can be used as a handle for further site-specific labeling in vitro. Here we provide protocols for in vivo N-terminal tagging of recombinant protein, and the synthesis and application of multifunctional reagents that enable protein labeling via click chemistry for affinity purification and detection by fluorescence. In addition to general N-terminal protein labeling, the protocol would be of particular use in providing evidence for native myristoylation of proteins of interest, proof of activity/selectivity of NMTs and cross-species reactivity of NMTs without resorting to the use of radioactive isotopes.
Indexed as
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22193303What OpenQuestion holds
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.