Kinetic model of in vivo folding and inclusion body formation in recombinant Escherichia coli (Q43514492)

24 November 2017

Kinetic model of in vivo folding and inclusion body formation in recombinant Escherichia coli (English)

1 reference

24 November 2017

1 reference

Hoffmann F

1

1 reference

PubMed ID

11135201

24 November 2017

Posten C

series ordinal

2

1 reference

PubMed ID

11135201

24 November 2017

Rinas U

series ordinal

3

1 reference

24 November 2017

1 February 2001

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Biotechnology and Bioengineering

24 November 2017

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24 November 2017

72

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24 November 2017

3

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24 November 2017

315-322

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Improved oligonucleotide site-directed mutagenesis using M13 vectors.

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Limited in vivo proteolysis of aggregated proteins.

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In vitro growth of Alzheimer's disease beta-amyloid plaques displays first-order kinetics.

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Production of abnormal proteins in E. coli stimulates transcription of lon and other heat shock genes

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

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

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Engineered turns of a recombinant antibody improve its in vivo folding

21 January 2018

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Kinetics studies for the optimization of recombinant protein formation.

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Transient rates of synthesis of individual polypeptides in E. coli following temperature shifts

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The purification of eukaryotic polypeptides synthesized in Escherichia coli

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Growth-associated synthesis of recombinant human glucagon and human growth hormone in high-cell-density cultures of Escherichia coli.

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Transient aggregates in protein folding are easily mistaken for folding intermediates

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

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Dynamics of in vivo protein aggregation: building inclusion bodies in recombinant bacteria

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Proteolytic digestion of bacterial inclusion body proteins during dynamic transition between soluble and insoluble forms

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Folding kinetics of the all-beta-sheet protein human basic fibroblast growth factor, a structural homolog of interleukin-1beta

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Simple fed-batch technique for high cell density cultivation of Escherichia coli

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Response of Escherichia coli cell membranes to induction of lambda cl857 prophage by heat shock

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Global suppression of protein folding defects and inclusion body formation

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Temperature-induced production of recombinant human insulin in high-cell density cultures of recombinant Escherichia coli

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Formation of short-lived protein aggregates directly from the coil in two-state folding

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Conformational states bound by the molecular chaperones GroEL and secB: a hidden unfolding (annealing) activity

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Reconstitution of lactic dehydrogenase. Noncovalent aggregation vs. reactivation. 1. Physical properties and kinetics of aggregation

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ClpB cooperates with DnaK, DnaJ, and GrpE in suppressing protein aggregation. A novel multi-chaperone system from Escherichia coli

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10.1002/1097-0290(20010205)72:3<315::AID-BIT8>3.0.CO;2-G

21 January 2018

Identifiers

DOI

1 reference

24 November 2017

1 reference

PubMed ID

11135201