ArticleBiomolecules2020
Production of Circularly Permuted Caspase-2 for Affinity Fusion-Tag Removal: Cloning, Expression in
Article in Biomolecules, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 39 citations in OpenAlex.
- Application of a novel fusion tag system for enhanced soluble expression of recombinant proteins in Escherichia coli.BMC biotechnology · 2026Article
- Extracellular peptide production in Escherichia coli by inducible downregulation of lipoprotein Lpp via MicL sRNA.Applied microbiology and biotechnology · 2025Article
- Antimicrobial peptide plectasin recombinantly produced inJournal of bacteriology · 2025Article
- Caspase-Based Fusion Protein Technology: Substrate Cleavability Described by Computational Modeling and Simulation.Journal of chemical information and modeling · 2024Article
- A production platform for disulfide-bonded peptides in the periplasm of Escherichia coli.Microbial cell factories · 2024Article
- Modifications of the 5' region of the CASPONMicrobial cell factories · 2024Article
- Essential factors, advanced strategies, challenges, and approaches involved for efficient expression of recombinant proteins in Escherichia coli.Archives of microbiology · 2024Review
- Factors involved in heterologous expression of proteins in E. coli host.Archives of microbiology · 2023Review
- Fusion Tag Design Influences Soluble Recombinant Protein Production inInternational journal of molecular sciences · 2022Article
- Structure-Based Design and Biological Evaluation of Novel Caspase-2 Inhibitors Based on the Peptide AcVDVAD-CHO and the Caspase-2-Mediated Tau Cleavage Sequence YKPVD314.ACS pharmacology & translational science · 2022Article
- Article
- PROFICS: A bacterial selection system for directed evolution of proteases.The Journal of biological chemistry · 2021Article
- A comprehensive antigen production and characterisation study for easy-to-implement, specific and quantitative SARS-CoV-2 serotests.EBioMedicine · 2021Article
- EfficientJournal of chemical information and modeling · 2021Article
- Enhancing the promiscuity of a member of the Caspase protease family by rational design.Proteins · 2020Article
Corrections and comments
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Authors and funding
15 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Caspase-2 is the most specific protease of all caspases and therefore highly suitable as tag removal enzyme creating an authentic N-terminus of overexpressed tagged proteins of interest. The wild type human caspase-2 is a dimer of heterodimers generated by autocatalytic processing which is required for its enzymatic activity. We designed a circularly permuted caspase-2 (cpCasp2) to overcome the drawback of complex recombinant expression, purification and activation, cpCasp2 was constitutively active and expressed as a single chain protein. A 22 amino acid solubility tag and an optimized fermentation strategy realized with a model-based control algorithm further improved expression in
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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.