Found: 10
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In vivo oxidative protein folding can be facilitated by oxidation–reduction cycling.
- Published in:
- Molecular Microbiology, 2010, v. 75, n. 1, p. 13, doi. 10.1111/j.1365-2958.2009.06952.x
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- Article
Isolation of full-length IgG antibodies from combinatorial libraries expressed in the cytoplasm of Escherichia coli.
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- Nature Communications, 2023, v. 14, n. 1, p. 1, doi. 10.1038/s41467-023-39178-x
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- Article
Multi-Copy Repression of Serratia marcescens Nuclease Expression by dinI.
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- Current Microbiology, 2002, v. 44, n. 1, p. 44, doi. 10.1007/s00284-001-0072-y
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- Article
Efficient expression of full-length antibodies in the cytoplasm of engineered bacteria.
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- Nature Communications, 2015, v. 6, n. 8, p. 8072, doi. 10.1038/ncomms9072
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- Article
SHuffle, a novel Escherichia coli protein expression strain capable of correctly folding disulfide bonded proteins in its cytoplasm.
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- Microbial Cell Factories, 2012, v. 11, n. 1, p. 56, doi. 10.1186/1475-2859-11-56
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- Article
Correction to: Production and applications of fluorobody from redox-engineered Escherichia coli.
- Published in:
- 2023
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- Correction Notice
Production and applications of fluorobody from redox-engineered Escherichia coli.
- Published in:
- Applied Microbiology & Biotechnology, 2023, v. 107, n. 5/6, p. 1959, doi. 10.1007/s00253-023-12395-6
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- Publication type:
- Article
Improved production of Humira antibody in the genetically engineered Escherichia coli SHuffle, by co-expression of human PDI-GPx7 fusions.
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- Applied Microbiology & Biotechnology, 2020, v. 104, n. 22, p. 9693, doi. 10.1007/s00253-020-10920-5
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- Article
A useful epitope tag derived from maltose binding protein.
- Published in:
- Protein Science: A Publication of the Protein Society, 2021, v. 30, n. 6, p. 1235, doi. 10.1002/pro.4088
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- Publication type:
- Article
RNase E, the Major Player in mRNA Degradation, Is Down-Regulated in Escherichia coli during a Transient Growth Retardation (Diauxic Lag).
- Published in:
- Biological Chemistry, 1998, v. 379, n. 1, p. 33, doi. 10.1515/bchm.1998.379.1.33
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- Article