Protocol for preparing proteins with improved solubility by co-expressing with molecular chaperones in Escherichia coli. (Q53855190)

21 May 2018

title

Protocol for preparing proteins with improved solubility by co-expressing with molecular chaperones in Escherichia coli. (English)

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21 May 2018

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Ario de Marco

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21 May 2018

publication date

1 January 2007

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21 May 2018

published in

Nature Protocols

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21 May 2018

volume

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21 May 2018

issue

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21 May 2018

page(s)

2632-2639

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21 May 2018

Getting newly synthesized proteins into shape.

cites work

1 reference

https://api.crossref.org/works/10.1038%2FNPROT.2007.400

Protein misfolding and inclusion body formation in recombinant Escherichia coli cells overexpressing Heat-shock proteins.

31 March 2020

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Identification of in vivo substrates of the chaperonin GroEL

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The small heat-shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNPROT.2007.400

Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNPROT.2007.400

Small heat shock proteins, ClpB and the DnaK system form a functional triade in reversing protein aggregation

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNPROT.2007.400

Characterization of the aggregates formed during recombinant protein expression in bacteria

31 March 2020

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https://api.crossref.org/works/10.1038%2FNPROT.2007.400

GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNPROT.2007.400

Expression of correctly folded proteins in Escherichia coli

31 March 2020

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https://api.crossref.org/works/10.1038%2FNPROT.2007.400

Genetic dissection of the roles of chaperones and proteases in protein folding and degradation in the Escherichia coli cytosol

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNPROT.2007.400

Bacteria co-transformed with recombinant proteins and chaperones cloned in independent plasmids are suitable for expression tuning

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNPROT.2007.400

Chaperone-based procedure to increase yields of soluble recombinant proteins produced in E. coli

31 March 2020

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Native folding of aggregation-prone recombinant proteins in Escherichia coli by osmolytes, plasmid- or benzyl alcohol-overexpressed molecular chaperones

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNPROT.2007.400

Protein aggregation as bacterial inclusion bodies is reversible

31 March 2020

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Two-step metal affinity purification of double-tagged (NusA-His6) fusion proteins.

31 March 2020

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Dimerization properties of a Xenopus laevis kinesin-II carboxy-terminal stalk fragment

31 March 2020

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Effect of ethanol and low-temperature culture on expression of soybean lipoxygenase L-1 in Escherichia coli

31 March 2020

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Transient accumulation of potassium glutamate and its replacement by trehalose during adaptation of growing cells of Escherichia coli K-12 to elevated sodium chloride concentrations

31 March 2020

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https://api.crossref.org/works/10.1038%2FNPROT.2007.400

Dicarboxylic amino acids and glycine-betaine regulate chaperone-mediated protein-disaggregation under stress.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNPROT.2007.400

The solubility of recombinant proteins expressed in Escherichia coli is increased by otsA and otsB co-transformation.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNPROT.2007.400

31 March 2020

Identifiers

DOI

10.1038/NPROT.2007.400

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21 May 2018

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21 May 2018