ArticleFrontiers in bioengineering and biotechnology2025
Controllable intein splicing and N-terminal cleavage at mesophilic temperatures.
Article in Frontiers in bioengineering and biotechnology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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Who cites it
1 citing paper in PubMed.
- Regulation of N-terminal cleavage and splicing in mini-Ter DnaE-3 intein by E23G and R50Q mutations.Biotechnology letters · 2026Article
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7 authors.
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Abstract
Inteins (intervening proteins) interrupt host proteins and are removed through a protein splicing reaction that ligates adjacent N- and C-exteins. The ability of inteins to specifically rearrange peptide bonds has proven exceptionally useful in protein engineering, thus, methods to control intein activity are of considerable interest. One particularly useful application of inteins is for the removal of an affinity tag following purification of a target protein through N-terminal cleavage (NTC). Typically, extended incubation at high temperature (greater than 50°C) or with an external nucleophile (e.g., dithiothreitol) is required to drive NTC, conditions that compromise the folding of many target proteins. Here, we characterize a variant of the
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