(Q47847151)

6 February 2018

title

Refolding of recombinant proteins (English)

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6 February 2018

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Clark EDB

1

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6 February 2018

publication date

1 April 1998

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6 February 2018

Current Opinion in Biotechnology

published in

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6 February 2018

volume

9

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6 February 2018

page(s)

157-163

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6 February 2018

issue

2

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6 February 2018

Protein folding and intermediates

cites work

1 reference

https://api.crossref.org/works/10.1016%2FS0958-1669%2898%2980109-2

7 January 2021

Comparing the refolding and reoxidation of recombinant porcine growth hormone from a urea denatured state and from Escherichia coli inclusion bodies.

1 reference

https://api.crossref.org/works/10.1016%2FS0958-1669%2898%2980109-2

7 January 2021

Expression, purification and characterization of recombinant human proinsulin

1 reference

https://api.crossref.org/works/10.1016%2FS0958-1669%2898%2980109-2

7 January 2021

Purification of overproduced Escherichia coli RNA polymerase sigma factors by solubilizing inclusion bodies and refolding from Sarkosyl

1 reference

https://api.crossref.org/works/10.1016%2FS0958-1669%2898%2980109-2

7 January 2021

Correct disulfide pairing and efficient refolding of detergent-solubilized single-chain Fv proteins from bacterial inclusion bodies

1 reference

https://api.crossref.org/works/10.1016%2FS0958-1669%2898%2980109-2

7 January 2021

Pathway of detergent-mediated and peptide ligand-mediated refolding of heterodimeric class II major histocompatibility complex (MHC) molecules

1 reference

https://api.crossref.org/works/10.1016%2FS0958-1669%2898%2980109-2

7 January 2021

Effect of inclusion body contaminants on the oxidative renaturation of hen egg white lysozyme

1 reference

https://api.crossref.org/works/10.1016%2FS0958-1669%2898%2980109-2

7 January 2021

Investigation of refolding condition for Pseudomonas fluorescens lipase by response surface methodology.

1 reference

https://api.crossref.org/works/10.1016%2FS0958-1669%2898%2980109-2

7 January 2021

Human low density lipoprotein receptor fragment. Successful refolding of a functionally active ligand-binding domain produced in Escherichia coli

1 reference

https://api.crossref.org/works/10.1016%2FS0958-1669%2898%2980109-2

7 January 2021

Recombinant human TIMP-3 from Escherichia coli: synthesis, refolding, physico-chemical and functional insights.

1 reference

https://api.crossref.org/works/10.1016%2FS0958-1669%2898%2980109-2

7 January 2021

Production of correctly folded recombinant [13C, 15N]-enriched guinea pig [Val90]-alpha-lactalbumin.

1 reference

https://api.crossref.org/works/10.1016%2FS0958-1669%2898%2980109-2

7 January 2021

Renaturation, purification and characterization of recombinant Fab-fragments produced in Escherichia coli

1 reference

https://api.crossref.org/works/10.1016%2FS0958-1669%2898%2980109-2

7 January 2021

Chromatography for rapid buffer exchange and refolding of secretory leukocyte protease inhibitor

1 reference

https://api.crossref.org/works/10.1016%2FS0958-1669%2898%2980109-2

7 January 2021

Studies of the hydrodynamic volume changes that occur during refolding of lysozyme using size-exclusion chromatography.

1 reference

https://api.crossref.org/works/10.1016%2FS0958-1669%2898%2980109-2

7 January 2021

Protein refolding at high concentration using size-exclusion chromatography.

1 reference

https://api.crossref.org/works/10.1016%2FS0958-1669%2898%2980109-2

7 January 2021

Improved refolding of an immobilized fusion protein.

1 reference

https://api.crossref.org/works/10.1016%2FS0958-1669%2898%2980109-2

7 January 2021

In vitro folding of inclusion body proteins.

1 reference

https://api.crossref.org/works/10.1016%2FS0958-1669%2898%2980109-2

7 January 2021

Oxidative renaturation of lysozyme at high concentrations.

1 reference

https://api.crossref.org/works/10.1016%2FS0958-1669%2898%2980109-2

7 January 2021

Control of aggregation in protein refolding: the temperature-leap tactic

1 reference

https://api.crossref.org/works/10.1016%2FS0958-1669%2898%2980109-2

7 January 2021

Effective renaturation of denatured and reduced immunoglobulin G in vitro without assistance of chaperone

1 reference

https://api.crossref.org/works/10.1016%2FS0958-1669%2898%2980109-2

7 January 2021

Kinetic and equilibrium folding intermediates

1 reference

https://api.crossref.org/works/10.1016%2FS0958-1669%2898%2980109-2

7 January 2021

How important is the molten globule for correct protein folding?

1 reference

https://api.crossref.org/works/10.1016%2FS0958-1669%2898%2980109-2

7 January 2021

The specificity of protein aggregation [new; comment]

1 reference

https://api.crossref.org/works/10.1016%2FS0958-1669%2898%2980109-2

7 January 2021

A kinetic study of the competition between renaturation and aggregation during the refolding of denatured-reduced egg white lysozyme.

1 reference

https://api.crossref.org/works/10.1016%2FS0958-1669%2898%2980109-2

7 January 2021

Specific aggregation of partially folded polypeptide chains: the molecular basis of inclusion body composition.

1 reference

https://api.crossref.org/works/10.1016%2FS0958-1669%2898%2980109-2

7 January 2021

Oxidative renaturation of hen egg-white lysozyme. Folding vs aggregation

1 reference

https://api.crossref.org/works/10.1016%2FS0958-1669%2898%2980109-2

7 January 2021

Polymerization mechanism of polypeptide chain aggregation

1 reference

https://api.crossref.org/works/10.1016%2FS0958-1669%2898%2980109-2

7 January 2021

Engineered turns of a recombinant antibody improve its in vivo folding

1 reference

https://api.crossref.org/works/10.1016%2FS0958-1669%2898%2980109-2

7 January 2021

Disrupting the hydrophobic patches at the antibody variable/constant domain interface: improved in vivo folding and physical characterization of an engineered scFv fragment.

1 reference

https://api.crossref.org/works/10.1016%2FS0958-1669%2898%2980109-2

7 January 2021

Artificial chaperone-assisted refolding of denatured-reduced lysozyme: modulation of the competition between renaturation and aggregation

1 reference

https://api.crossref.org/works/10.1016%2FS0958-1669%2898%2980109-2

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0958-1669%2898%2980109-2

7 January 2021

Refolding with a piece of the ring

1 reference

https://api.crossref.org/works/10.1016%2FS0958-1669%2898%2980109-2

7 January 2021

Refolding chromatography with immobilized mini-chaperones

1 reference

https://api.crossref.org/works/10.1016%2FS0958-1669%2898%2980109-2

7 January 2021

Artificial chaperone-assisted refolding of carbonic anhydrase B

1 reference

https://api.crossref.org/works/10.1016%2FS0958-1669%2898%2980109-2

7 January 2021

Refolding of SDS- and thermally denatured MM-creatine kinase using cyclodextrins

1 reference

https://api.crossref.org/works/10.1016%2FS0958-1669%2898%2980109-2

7 January 2021

Control of aggregation in protein refolding: a variety of surfactants promote renaturation of carbonic anhydrase II.

1 reference

https://api.crossref.org/works/10.1016%2FS0958-1669%2898%2980109-2

7 January 2021

Effect of additives on the renaturation of reduced lysozyme in the presence of 4 M urea.

1 reference

https://api.crossref.org/works/10.1016%2FS0958-1669%2898%2980109-2

7 January 2021

Non-detergent sulphobetaines: a new class of molecules that facilitate in vitro protein renaturation

1 reference

https://api.crossref.org/works/10.1016%2FS0958-1669%2898%2980109-2

7 January 2021

Molten globule intermediate of recombinant human growth hormone: stabilization with surfactants

1 reference

https://api.crossref.org/works/10.1016%2FS0958-1669%2898%2980109-2

7 January 2021

10.1016/S0958-1669(98)80109-2

Identifiers

DOI

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6 February 2018

PubMed ID

9664053

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6 February 2018