Effect of temperature on protein quality in bacterial inclusion bodies (Q42603326)

3 November 2017

title

Effect of temperature on protein quality in bacterial inclusion bodies (English)

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3 November 2017

Natalia Sánchez de Groot

series ordinal

1

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author name string

Salvador Ventura

series ordinal

2

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3 November 2017

language of work or name

English

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publication date

10 November 2006

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3 November 2017

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volume

580

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3 November 2017

issue

27

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3 November 2017

page(s)

6471-6476

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Recombinant protein folding and misfolding in Escherichia coli

3 November 2017

cites work

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2006.10.071

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Aggregation as bacterial inclusion bodies does not imply inactivation of enzymes and fluorescent proteins

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Kinetics of inclusion body formation studied in intact cells by FT-IR spectroscopy.

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Protein quality in bacterial inclusion bodies.

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High activity of inclusion bodies formed in Escherichia coli overproducing Clostridium thermocellum endoglucanase D.

21 January 2018

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Protein activity in bacterial inclusion bodies correlates with predicted aggregation rates.

21 January 2018

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Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli

21 January 2018

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The evaluation of the factors that cause aggregation during recombinant expression in E. coli is simplified by the employment of an aggregation-sensitive reporter.

21 January 2018

1 reference

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Temperature effect on inclusion body formation and stress response in the periplasm of Escherichia coli

21 January 2018

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Fine architecture of bacterial inclusion bodies

21 January 2018

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

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Mutagenesis of the central hydrophobic cluster in Abeta42 Alzheimer's peptide. Side-chain properties correlate with aggregation propensities

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Protein aggregation in vitro and in vivo: a quantitative model of the kinetic competition between folding and aggregation

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Temperature, stability, and the hydrophobic interaction

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Annealing prion protein amyloid fibrils at high temperature results in extension of a proteinase K-resistant core.

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Production of nonclassical inclusion bodies from which correctly folded protein can be extracted

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Secondary structure characterization of beta-lactamase inclusion bodies.

21 January 2018

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Amyloid-like properties of bacterial inclusion bodies.

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Sequence determinants of protein aggregation: tools to increase protein solubility

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Solubilization and refolding of bacterial inclusion body proteins

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Characterization of the aggregates formed during recombinant protein expression in bacteria

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Optimization of Inclusion Body Solubilization and Renaturation of Recombinant Human Growth Hormone from Escherichia coli

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Identifiers

DOI

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3 November 2017

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