ArticleBioorganic & medicinal chemistry2021
Site-specific covalent labeling of His-tag fused proteins with N-acyl-N-alkyl sulfonamide reagent.
Article in Bioorganic & medicinal chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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The trial behind it
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
10 citing papers in PubMed.
- Progress and challenges in traceless ligand-directed labelling chemistry.Communications chemistry · 2026Review
- Recent advances in site-specific modifications of peptides and proteins.Chemical science · 2026Review
- Expediated synthesis ofOrganic & biomolecular chemistry · 2026Article
- N-Acyl-N-Alkyl Sulfonamide Mediated Bioconjugation ofHis-Tag Fused Proteins.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Peptide Tags for Site-Selective Nonenzymatic Covalent Modification of Proteins.Journal of peptide science : an official publication of the European Peptide Society · 2025Review
- Advancing Single-Molecule Biophysics: Next-Generation Organic Fluorophores with Tailored Labeling Strategies.Chemical & biomedical imaging · 2025Review
- Advancing Covalent Ligand and Drug Discovery beyond Cysteine.Chemical reviews · 2025Review
- Cell Surface Labeling and Detection of Protein Tyrosine Kinase 7 via Covalent Aptamers.Journal of the American Chemical Society · 2023Article
- Site-Selective Incorporation of a Functional Group into Lys175 in the Vicinity of the Active Site of Chymotrypsin by Using Peptidyl α-Aminoalkylphosphonate Diphenyl Ester-Derivatives.Molecules (Basel, Switzerland) · 2023Article
- Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
The ability to incorporate a desired functionality into proteins of interest in a site-specific manner can provide powerful tools for investigating biological systems and creating therapeutic conjugates. However, there are not any universal methods that can be applied to all proteins, and it is thus important to explore the chemical strategy for protein modification. In this paper, we developed a new reactive peptide tag/probe pair system for site-specific covalent protein labeling. This method relies on the recognition-driven reaction of a peptide tag and a molecular probe, which comprises the lysine-containing short histidine tag (KH6 or H6K) and a binuclear nickel (II)- nitrilotriacetic acid (Ni
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Registered trials
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