ArticleBioconjugate chemistry2020
Efficient Sortase-Mediated Ligation Using a Common C-Terminal Fusion Tag.
Article in Bioconjugate chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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.
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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, 28 citations in OpenAlex.
- Article
- Exploiting Selective Position Labeling to Unveil the Hidden Complexity of Terminomics.Molecules (Basel, Switzerland) · 2026Review
- Application of Sortase-Mediated Ligation for the Synthesis of Block Copolymers and Protein-Polymer Conjugates.Macromolecular bioscience · 2025Article
- Leveraging immunoliposomes as nanocarriers against SARS-CoV-2 and its emerging variants.Asian journal of pharmaceutical sciences · 2023Review
- Challenges in the use of sortase and other peptide ligases for site-specific protein modification.Chemical Society reviews · 2022Review
- Optimized Production of Fc Fusion Proteins by Sortase Enzymatic Ligation.Industrial & engineering chemistry research · 2021Article
- A modular toolbox to generate complex polymeric ubiquitin architectures using orthogonal sortase enzymes.Nature communications · 2021Article
- Engineered Sortases in Peptide and Protein Chemistry.Chembiochem : a European journal of chemical biology · 2021Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Sortase-mediated ligation is a powerful method for generating site-specifically modified proteins. However, this process is limited by the inherent reversibility of the ligation reaction. To address this, here we report the continued development and optimization of an experimentally facile strategy for blocking reaction reversibility. This approach, which we have termed metal-assisted sortase-mediated ligation (MA-SML), relies on the use of a solution additive (Ni
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Registered trials
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