ArticleApplied and environmental microbiology2022
An Intrinsically Disordered Peptide Tag that Confers an Unusual Solubility to Aggregation-Prone Proteins.
Article in Applied and environmental microbiology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 30 citations in OpenAlex.
- Engineering of a Carbonic Anhydrase fromInternational journal of molecular sciences · 2026Article
- A standardized set of pNX vectors for enhanced soluble expression of recombinant proteins in E. coli using small fusion tags.Microbial cell factories · 2025Article
- Development and Functional Characterization of Recombinant Mussel Adhesive Protein for Anti-Oxidative and Anti-Aging Therapeutic Applications.International journal of molecular sciences · 2025Article
- Further characterization and engineering of an 11-amino acid motif for enhancing recombinant soluble protein expression.Microbial cell factories · 2025Article
- Recent advances in recombinant production of soluble proteins in E. coli.Microbial cell factories · 2025Review
- Recombinant multiepitope proteins expressed in Escherichia coli cells and their potential for immunodiagnosis.Microbial cell factories · 2024Review
- Synthetic intrinsically disordered protein fusion tags that enhance protein solubility.Nature communications · 2024Article
- Protein structure-function continuum model: Emerging nexuses between specificity, evolution, and structure.Protein science : a publication of the Protein Society · 2024Review
- Essential factors, advanced strategies, challenges, and approaches involved for efficient expression of recombinant proteins in Escherichia coli.Archives of microbiology · 2024Review
- Improved Solubility and Stability of a Thermostable Carbonic Anhydrase via Fusion with Marine-Derived Intrinsically Disordered Solubility Enhancers.International journal of molecular sciences · 2024Article
- Factors involved in heterologous expression of proteins in E. coli host.Archives of microbiology · 2023Review
- Article
- Strategies for efficient production of recombinant proteins in Escherichia coli: alleviating the host burden and enhancing protein activity.Microbial cell factories · 2022Review
- Enhanced Production of a Thermostable Carbonic Anhydrase inMolecules (Basel, Switzerland) · 2021Article
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
There is a high demand for the production of recombinant proteins in Escherichia coli for biotechnological applications, but their production is still limited by their insolubility. Fusion tags have been successfully used to enhance the solubility of aggregation-prone proteins; however, smaller and more powerful tags are desired for increasing the yield and quality of target proteins. Here, the NEXT tag, a 53-amino-acid-long solubility enhancer, is described. The NEXT tag showed outstanding ability to improve both
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Registered trials
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