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In vitro protein refolding by chromatographic procedures
Open accessAbstract
In vitro protein refolding is still a bottleneck in both structural biology and in the development of new biopharmaceuticals, especially for commercially important polypeptides that are overexpressed in Escherichia coli. This review focuses on protein refolding methods based on column procedures because recent advances in chromatographic refolding have shown promising results.
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Cited by
Protein recovery from inclusion bodies of Escherichia coli using mild solubilization process
Singh, A., Upadhyay, V., Upadhyay, A. K., Singh, S. M., & Panda, A. K. (2015) · Microbial Cell Factories · doi:10.1186/s12934-015-0222-8 · Cited by 444
Protein quality in bacterial inclusion bodies
Ventura, S., & Villaverde, A. (2006) · Trends in Biotechnology · doi:10.1016/j.tibtech.2006.02.007 · Cited by 381
Refolding Techniques for Recovering Biologically Active Recombinant Proteins from Inclusion Bodies
Yamaguchi, H., & Miyazaki, M. (2014) · Biomolecules · doi:10.3390/biom4010235 · Cited by 251
Refolding of proteins from inclusion bodies: rational design and recipes
Basu, A., Li, X., & Leong, S. S. J. (2011) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-011-3513-y · Cited by 79
Metadata
- Authors
- Li, M., Su, Z.-G., & Janson, J.-C.
- Venue
- Protein Expression and Purification
- Publisher
- Elsevier BV
- Published
- 2004-01
- Volume
- 33
- Issue
- 1
- Pages
- 1-10
- ISSN
- 1046-5928 (ISSN-L)
- OpenAlex
- W2145250917
- Cited by
- 191
- References
- 0
- FWCI
- 3.75
- Type
- journal article
- Language
- en
- Open access
- green
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