Native folding of aggregation-prone recombinant proteins in Escherichia coli by osmolytes, plasmid- or benzyl alcohol-overexpressed molecular chaperones (Q34133518)

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Language	Label	Description	Also known as
English	Native folding of aggregation-prone recombinant proteins in Escherichia coli by osmolytes, plasmid- or benzyl alcohol-overexpressed molecular chaperones	scientific article

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

31 July 2017

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

1 reference

Europe PubMed Central

PubMed publication ID

31 July 2017

protein folding

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Escherichia coli

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molecular chaperones

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1 reference

based on heuristic

inferred from title

author name string

Ario de Marco

1

1 reference

Europe PubMed Central

PubMed publication ID

31 July 2017

Laszlo Vigh

2

1 reference

Europe PubMed Central

PubMed publication ID

31 July 2017

Sophia Diamant

3

1 reference

Europe PubMed Central

PubMed publication ID

31 July 2017

Pierre Goloubinoff

4

1 reference

Europe PubMed Central

PubMed publication ID

31 July 2017

publication date

1 January 2005

1 reference

Europe PubMed Central

PubMed publication ID

31 July 2017

Cell Stress & Chaperones

1 reference

Europe PubMed Central

PubMed publication ID

31 July 2017

10

1 reference

Europe PubMed Central

PubMed publication ID

31 July 2017

4

1 reference

Europe PubMed Central

PubMed publication ID

31 July 2017

329-339

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Europe PubMed Central

PubMed publication ID

31 July 2017

Characterization of the aggregates formed during recombinant protein expression in bacteria

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1283876

28 July 2018

Recombinant protein folding and misfolding in Escherichia coli

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1283876

28 July 2018

sHsps and their role in the chaperone network

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1283876

28 July 2018

Preparative protein refolding

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1283876

28 July 2018

Review: mechanisms of disaggregation and refolding of stable protein aggregates by molecular chaperones

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1283876

28 July 2018

Synechocystis HSP17 is an amphitropic protein that stabilizes heat-stressed membranes and binds denatured proteins for subsequent chaperone-mediated refolding

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1283876

28 July 2018

Protein aggregation as bacterial inclusion bodies is reversible

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1283876

28 July 2018

Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1283876

28 July 2018

Membrane physical state controls the signaling mechanism of the heat shock response in Synechocystis PCC 6803: identification of hsp17 as a "fluidity gene".

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1283876

28 July 2018

Expression of eukaryotic proteins in soluble form in Escherichia coli

1 reference

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28 July 2018

Strategies for optimizing heterologous protein expression in Escherichia coli

1 reference

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28 July 2018

Stable transformation of an Arabidopsis cell suspension culture with firefly luciferase providing a cellular system for analysis of chaperone activity in vivo

1 reference

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28 July 2018

Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1283876

28 July 2018

Strategies for achieving high-level expression of genes in Escherichia coli

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1283876

28 July 2018

Expression of correctly folded proteins in Escherichia coli

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1283876

28 July 2018

The formation and stabilization of protein structure

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1283876

28 July 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1283876

28 July 2018

Controlled expression of recombinant proteins in Physcomitrella patens by a conditional heat-shock promoter: a tool for plant research and biotechnology

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1283876

28 October 2018

Fusion tags and chaperone co-expression modulate both the solubility and the inclusion body features of the recombinant CLIPB14 serine protease

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1283876

28 October 2018

Amyloid-like properties of bacterial inclusion bodies.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1283876

28 October 2018

Membrane fluidization triggers membrane remodeling which affects the thermotolerance in Escherichia coli.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1283876

28 October 2018

Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1283876

28 October 2018

The solubility and stability of recombinant proteins are increased by their fusion to NusA.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1283876

28 October 2018

Active solubilization and refolding of stable protein aggregates by cooperative unfolding action of individual hsp70 chaperones

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1283876

28 October 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1283876

28 October 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1283876

28 October 2018

Medium-scale structural genomics: strategies for protein expression and crystallization

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1283876

28 October 2018

In vivo aggregation of a single enzyme limits growth of Escherichia coli at elevated temperatures

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1283876

28 October 2018

Proteinaceous infectious behavior in non-pathogenic proteins is controlled by molecular chaperones.

1 reference

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28 October 2018

Production of functional single-chain Fv antibodies in the cytoplasm of Escherichia coli

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1283876

28 October 2018

Chemical chaperones regulate molecular chaperones in vitro and in cells under combined salt and heat stresses

1 reference

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28 October 2018

A strategy for optimizing the monodispersity of fusion proteins: application to purification of recombinant HPV E6 oncoprotein

1 reference

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28 October 2018

Size-dependent disaggregation of stable protein aggregates by the DnaK chaperone machinery.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1283876

28 October 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1283876

28 October 2018

Chaperonin function: folding by forced unfolding

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1283876

28 October 2018

Properties of soluble fusions between mammalian aspartic proteinases and bacterial maltose-binding protein.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1283876

28 October 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1283876

28 October 2018

High-Level Expression of Soluble Protein inEscherichia coliUsing a His6-Tag and Maltose-Binding-Protein Double-Affinity Fusion System

1 reference

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A thioredoxin gene fusion expression system that circumvents inclusion body formation in the E. coli cytoplasm.

1 reference

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A modular polycistronic expression system for overexpressing protein complexes in Escherichia coli

1 reference

https://pubmed.ncbi.nlm.nih.gov/16333986

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1 reference

https://pubmed.ncbi.nlm.nih.gov/16333986

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Formation of soluble inclusion bodies by hpv e6 oncoprotein fused to maltose-binding protein

1 reference

https://pubmed.ncbi.nlm.nih.gov/16333986

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/16333986

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/16333986

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/16333986

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based on heuristic

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/16333986

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Refolding of Escherichia coli produced membrane protein inclusion bodies immobilised by nickel chelating chromatography

1 reference

https://pubmed.ncbi.nlm.nih.gov/16333986

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Does the membrane's physical state control the expression of heat shock and other genes?

1 reference

https://pubmed.ncbi.nlm.nih.gov/16333986

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Isolation of tobacco isoperoxidases accumulated in cell-suspension culture medium and characterization of activities related to cell wall metabolism

1 reference

https://pubmed.ncbi.nlm.nih.gov/16333986

12 December 2020

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Identifiers

10.1379/CSC-139R.1

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Europe PubMed Central

PubMed publication ID

31 July 2017

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PMC publication ID

1 reference

Europe PubMed Central

PubMed publication ID

31 July 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

31 July 2017

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