ArticleAngewandte Chemie (International ed. in English)2017
Proximity-Based Sortase-Mediated Ligation.
Article in Angewandte Chemie (International ed. in English), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
What it found
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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.
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
31 citing papers in PubMed.
- A Putative Interaction between the Transmembrane Domains ofThe journal of physical chemistry. B · 2025Article
- Synthetic protein degradation circuits using programmable cleavage and ligation by Sortase A.Nature communications · 2025Article
- Development of a Versatile Cancer Vaccine Format Targeting Antigen-Presenting Cells Using Proximity-Based Sortase A-Mediated Ligation of T-Cell Epitopes.Bioconjugate chemistry · 2024Article
- Sortase mediated protein ubiquitination with defined chain length and topology.RSC chemical biology · 2024Article
- Intracellular Protein Delivery: Approaches, Challenges, and Clinical Applications.BME frontiers · 2024Review
- Lipid Nanoparticle Delivery of Small Proteins for PotentACS applied materials & interfaces · 2023Article
- Nature-inspired protein ligation and its applications.Nature reviews. Chemistry · 2023Review
- Enzymatic Construction of DARPin-Based Targeted Delivery Systems Using Protein Farnesyltransferase and a Capture and Release Strategy.International journal of molecular sciences · 2022Article
- Challenges in the use of sortase and other peptide ligases for site-specific protein modification.Chemical Society reviews · 2022Review
- Rapid, site-specific labeling of "off-the-shelf" and native serum autoantibodies with T cell-redirecting domains.Science advances · 2022Article
- Cytosolic Delivery of Small Protein Scaffolds Enables Efficient Inhibition of Ras and Myc.Molecular pharmaceutics · 2022Article
- Design of fusion enzymes for biocatalytic applications in aqueous and non-aqueous media.Frontiers in bioengineering and biotechnology · 2022Review
- Protein scaffolds: A tool for multi-enzyme assembly.Biotechnology reports (Amsterdam, Netherlands) · 2021Review
- Recent progress in mass spectrometry-based strategies for elucidating protein-protein interactions.Cellular and molecular life sciences : CMLS · 2021Review
- Efficient Labeling of Native Human IgG by Proximity-Based Sortase-Mediated Isopeptide Ligation.Bioconjugate chemistry · 2021Article
- Quantitative interrogation of protein co-aggregation using multi-color fluorogenic protein aggregation sensors.Chemical science · 2021Article
- Engineered Sortases in Peptide and Protein Chemistry.Chembiochem : a European journal of chemical biology · 2021Review
- Site-Specific Modification of Single-Chain Affinity Ligands for Fluorescence Labeling, Radiolabeling, and Bioconjugation.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Power to the protein: enhancing and combining activities using the Spy toolbox.Chemical science · 2020Review
- Engineered peptide ligases for cell signaling and bioconjugation.Biochemical Society transactions · 2020Review
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Protein bioconjugation has been a crucial tool for studying biological processes and developing therapeutics. Sortase A (SrtA), a bacterial transpeptidase, has become widely used for its ability to site-specifically label proteins with diverse functional moieties, but a significant limitation is its poor reaction kinetics. In this work, we address this by developing proximity-based sortase-mediated ligation (PBSL), which improves the ligation efficiency to over 95 % by linking the target protein to SrtA using the SpyTag-SpyCatcher peptide-protein pair. By expressing the target protein with SpyTag C-terminal to the SrtA recognition motif, it can be covalently captured by an immobilized SpyCatcher-SrtA fusion protein during purification. Following the ligation reaction, SpyTag is cleaved off, rendering PBSL traceless, and only the labeled protein is released, simplifying target protein purification and labeling to a single step.
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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.