Molecular chaperones, folding catalysts, and the recovery of active recombinant proteins from E. coli. To fold or to refold (Q41581093)

4 October 2017

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title

Molecular chaperones, folding catalysts, and the recovery of active recombinant proteins from E. coli. To fold or to refold (English)

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4 October 2017

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Thomas JG

1

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4 October 2017

Ayling A

series ordinal

2

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4 October 2017

Baneyx F

series ordinal

3

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4 October 2017

language of work or name

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1 June 1997

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Applied Biochemistry and Biotechnology

4 October 2017

published in

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4 October 2017

volume

66

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4 October 2017

issue

3

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4 October 2017

page(s)

197-238

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The purification of eukaryotic polypeptides synthesized in Escherichia coli

4 October 2017

cites work

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https://api.crossref.org/works/10.1007%2FBF02785589

The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FBF02785589

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FBF02785589

Expression and characterization of branched-chain alpha-ketoacid dehydrogenase kinase from the rat. Is it a histidine-protein kinase?

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FBF02785589

Purification and characterization of the heat shock proteins HslV and HslU that form a new ATP-dependent protease in Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FBF02785589

Eukaryotic protein disulfide isomerase complements Escherichia coli dsbA mutants and increases the yield of a heterologous secreted protein with disulfide bonds.

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FBF02785589

Human protein disulfide isomerase functionally complements a dsbA mutation and enhances the yield of pectate lyase C in Escherichia coli.

21 January 2018

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https://api.crossref.org/works/10.1007%2FBF02785589

A novel function of Escherichia coli chaperone DnaJ. Protein-disulfide isomerase.

21 January 2018

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https://api.crossref.org/works/10.1007%2FBF02785589

Refolding and release of tubulins by a functional immobilized groEL column.

21 January 2018

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https://api.crossref.org/works/10.1007%2FBF02785589

Co-overexpression of bacterial GroESL chaperonins partly overcomes non-productive folding and tetramer assembly of E. coli-expressed human medium-chain acyl-CoA dehydrogenase (MCAD) carrying the prevalent disease-causing K304E mutation.

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FBF02785589

Engineering and overexpression of periplasmic forms of the penicillin-binding protein 3 of Escherichia coli

21 January 2018

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https://api.crossref.org/works/10.1007%2FBF02785589

Escherichia coli chaperonins cpn60 (groEL) and cpn10 (groES) do not catalyse the refolding of mitochondrial malate dehydrogenase

21 January 2018

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https://api.crossref.org/works/10.1007%2FBF02785589

Calf thymus Hsc70 protein protects and reactivates prokaryotic and eukaryotic enzymes.

21 January 2018

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https://api.crossref.org/works/10.1007%2FBF02785589

Structure and in vitro molecular chaperone activity of cytosolic small heat shock proteins from pea.

21 January 2018

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https://api.crossref.org/works/10.1007%2FBF02785589

21 January 2018

Identifiers

DOI

10.1007/BF02785589

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Dimensions Publication ID

4 October 2017

1027783687

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