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Literature DB >> 17621288

Recombinant protein solubility - does more mean better?

Nuria González-Montalbán, Elena García-Fruitós, Antonio Villaverde.

Abstract

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Year: 2007 PMID： 17621288 DOI： 10.1038/nbt0707-718

Source DB: PubMed Journal: Nat Biotechnol ISSN： 1087-0156 Impact factor: 54.908

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40 in total

1. Disulfide bond formation and activation of Escherichia coli β-galactosidase under oxidizing conditions.

Authors: Joaquin Seras-Franzoso; Roman Affentranger; Mario Ferrer-Navarro; Xavier Daura; Antonio Villaverde; Elena García-Fruitós
Journal: Appl Environ Microbiol Date: 2012-01-27 Impact factor: 4.792

2. Production of recombinant proteins in the lon-deficient BL21(DE3) strain of Escherichia coli in the absence of the DnaK chaperone.

Authors: Julien Ratelade; Marie-Caroline Miot; Emmett Johnson; Jean-Michel Betton; Philippe Mazodier; Nadia Benaroudj
Journal: Appl Environ Microbiol Date: 2009-04-03 Impact factor: 4.792

3. Inclusion bodies: a new concept.

Authors: Elena García-Fruitós
Journal: Microb Cell Fact Date: 2010-11-01 Impact factor: 5.328

4. The Functional quality of soluble recombinant polypeptides produced in Escherichia coli is defined by a wide conformational spectrum.

Authors: Mónica Martínez-Alonso; Nuria González-Montalbán; Elena García-Fruitós; Antonio Villaverde
Journal: Appl Environ Microbiol Date: 2008-10-03 Impact factor: 4.792

Recombinant protein solubility - does more mean better?

1. Disulfide bond formation and activation of Escherichia coli β-galactosidase under oxidizing conditions.

2. Production of recombinant proteins in the lon-deficient BL21(DE3) strain of Escherichia coli in the absence of the DnaK chaperone.

3. Inclusion bodies: a new concept.

4. The Functional quality of soluble recombinant polypeptides produced in Escherichia coli is defined by a wide conformational spectrum.

Review 5. Towards revealing the structure of bacterial inclusion bodies.

6. Rehosting of bacterial chaperones for high-quality protein production.

7. Cross-system excision of chaperone-mediated proteolysis in chaperone-assisted recombinant protein production.

8. Influence of production process design on inclusion bodies protein: the case of an Antarctic flavohemoglobin.

Review 9. Side effects of chaperone gene co-expression in recombinant protein production.

10. Isolation of cell-free bacterial inclusion bodies.