The DOI matches its Crossref record; 148 of the 148 references it cites were found in a registry or an index.
Strategies to Optimize Protein Expression in E. coli
Open accessAbstract
Recombinant protein expression inEscherichia coli(E. coli) is simple, fast, inexpensive, and robust, with the expressed protein comprising up to 50 percent of the total cellular protein. However, it also has disadvantages. For example, the rapidity of bacterial protein expression often results in unfolded/misfolded proteins, especially for heterologous proteins that require longer times and/or molecular chaperones to fold correctly. In addition, the highly reductive environment of the bacterial cytosol and the inability ofE. colito perform several eukaryotic post‐translational modifications results in the insoluble expression of proteins that require these modifications for folding and activity. Fortunately, multiple, novel reagents and techniques have been developed that allow for the efficient, soluble production of a diverse range of heterologous proteins inE. coli. This overview describes variables at each stage of a protein expression experiment that can influence solubility and offers a summary of strategies used to optimize soluble expression inE. coli.Curr. Protoc. Protein Sci. 61:5.24.1‐5.24.29. © 2010 by John Wiley & Sons, Inc.
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1 retracted
A New Strategy for the Synthesis of Glycoproteins
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Cited by
Jia, B., & Jeon, C. O. (2016) · Open Biology · doi:10.1098/rsob.160196 · Cited by 295
Cryo-EM structure of the HIV-1 Pol polyprotein provides insights into virion maturation
Harrison, J. J. E. K., Passos, D. O., Bruhn, J. F., Bauman, J. D., Tuberty, L., DeStefano, J. J., Ruiz, F. X., Lyumkis, D., & Arnold, E. (2022) · Science Advances · doi:10.1126/sciadv.abn9874 · Cited by 31
Metadata
- Authors
- Francis, D. M., & Page, R.
- Venue
- Current Protocols in Protein Science
- Publisher
- Wiley
- Published
- 2010-08
- Volume
- 61
- Issue
- 1
- Pages
- 5.24.1-5.24.29
- ISSN
- 1934-3655 (ISSN-L)
- 1934-3663
- OpenAlex
- W1682566403
- Cited by
- 272
- References
- 148
- FWCI
- 2.01
- Type
- journal article
- Language
- en
- Open access
- bronze
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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