ArticleJournal of molecular biology2009
Selection and structure of hyperactive inteins: peripheral changes relayed to the catalytic center.
Article in Journal of molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
What it found
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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
23 citing papers in PubMed.
- Regulation of N-terminal cleavage and splicing in mini-Ter DnaE-3 intein by E23G and R50Q mutations.Biotechnology letters · 2026Article
- Article
- Efficient splicing of the CPE intein derived from directed evolution of theActa biochimica et biophysica Sinica · 2023Article
- SufB intein splicing in Mycobacterium tuberculosis is influenced by two remote conserved N-extein histidines.Bioscience reports · 2022Article
- An alternative domain-swapped structure of the Pyrococcus horikoshii PolII mini-intein.Scientific reports · 2021Article
- Intein Inhibitors as Novel Antimicrobials: Protein Splicing in Human Pathogens, Screening Methods, and Off-Target Considerations.Frontiers in molecular biosciences · 2021Review
- Protein Splicing Activity of theBiochemistry · 2020Article
- Allosteric Influence of Extremophile Hairpin Motif Mutations on the Protein Splicing Activity of a Hyperthermophilic Intein.Biochemistry · 2020Article
- Structure of an engineered intein reveals thiazoline ring and provides mechanistic insight.Biotechnology and bioengineering · 2019Article
- Conditional Protein Splicing Switch in Hyperthermophiles through an Intein-Extein Partnership.mBio · 2018Article
- Full and Partial Agonism of a Designed Enzyme Switch.ACS synthetic biology · 2016Article
- Backbone assignments of mini-RecA intein with short native exteins and an active N-terminal catalytic cysteine.Biomolecular NMR assignments · 2015Article
- Dynamics differentiate between active and inactive inteins.European journal of medicinal chemistry · 2015Article
- Structural and dynamical features of inteins and implications on protein splicing.The Journal of biological chemistry · 2014Review
- Inteins: Nature's Gift to Protein Chemists.Chemical science · 2014Article
- Recent progress in intein research: from mechanism to directed evolution and applications.Cellular and molecular life sciences : CMLS · 2013Review
- Structured crowding and its effects on enzyme catalysis.Topics in current chemistry · 2013Review
- Unprecedented rates and efficiencies revealed for new natural split inteins from metagenomic sources.The Journal of biological chemistry · 2012Article
- Highly efficient and more general cis- and trans-splicing inteins through sequential directed evolution.The Journal of biological chemistry · 2011Article
- pK(a) coupling at the intein active site: implications for the coordination mechanism of protein splicing with a conserved aspartate.Journal of the American Chemical Society · 2011Article
Corrections and comments
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Authors and funding
10 authors.
Funding
Abstract
Inteins are phylogenetically diverse self-splicing proteins that are of great functional, evolutionary, biotechnological, and medical interest. To address the relationship between intein structure and function, particularly with respect to regulating the splicing reaction, and to groom inteins for application, we developed a phage display system to extend current in vivo selection for enhanced intein function to selection in vitro. We thereby isolated inteins that can function under excursions in temperature, pH, and denaturing environment. Remarkably, most mutations mapped to the surface of the intein, remote from the active site. We chose two mutants with enhanced splicing activity for crystallography, one of which was also subjected to NMR analysis. These studies define a "ripple effect", whereby mutations in peripheral non-catalytic residues can cause subtle allosteric changes in the active-site environment in a way that facilitates intein activity. Altered salt-bridge formation and chemical shift changes of the mutant inteins provide a molecular rationale for their phenotypes. These fundamental insights will advance the utility of inteins in chemical biology, biotechnology, and medicine.
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Registered trials
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