Cargando…
mRNA Engineering for the Efficient Chaperone-Mediated Co-Translational Folding of Recombinant Proteins in Escherichia coli
The production of soluble, functional recombinant proteins by engineered bacterial hosts is challenging. Natural molecular chaperone systems have been used to solubilize various recombinant proteins with limited success. Here, we attempted to facilitate chaperone-mediated folding by directing the mo...
Autores principales: | Bui, Le Minh, Geraldi, Almando, Nguyen, Thi Thuy, Lee, Jun Hyoung, Lee, Ju Young, Cho, Byung-Kwan, Kim, Sun Chang |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2019
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6651523/ https://www.ncbi.nlm.nih.gov/pubmed/31261687 http://dx.doi.org/10.3390/ijms20133163 |
Ejemplares similares
-
Enhanced Production of Fatty Acid Ethyl Ester with Engineered fabHDG Operon in Escherichia coli
por: Rahman, Ziaur, et al.
Publicado: (2019) -
Synthetic Scaffold Systems for Increasing the Efficiency of Metabolic Pathways in Microorganisms
por: Geraldi, Almando, et al.
Publicado: (2021) -
Exploring the Potential of a Genome-Reduced Escherichia coli Strain for Plasmid DNA Production
por: Nguyen, Thi Thuy, et al.
Publicado: (2023) -
Chaperone-mediated native folding of a β-scorpion toxin in the periplasm of Escherichia coli()
por: O'Reilly, A.O., et al.
Publicado: (2014) -
Production of Indigo by Recombinant Escherichia coli with Expression of Monooxygenase, Tryptophanase, and Molecular Chaperone
por: Du, Lingyan, et al.
Publicado: (2022)