(Q35520931)

English

Co-production of GroELS discriminates between intrinsic and thermally-induced recombinant protein aggregation during substrate quality control

scientific article published on 12 October 2011

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

8 August 2017

Co-production of GroELS discriminates between intrinsic and thermally-induced recombinant protein aggregation during substrate quality control (English)

1 reference

Europe PubMed Central

PubMed publication ID

8 August 2017

quality control

0 references

protein aggregation

1 reference

based on heuristic

inferred from title

Olivia Cano-Garrido

object named as

Olivia Cano-Garrido

4

0 references

Elena García-Fruitós

object named as

Elena García-Fruitós

3

0 references

Antonio Villaverde

object named as

Antonio Villaverde

5

0 references

author name string

Gemma Platas

1

1 reference

Europe PubMed Central

PubMed publication ID

8 August 2017

Escarlata Rodríguez-Carmona

2

1 reference

Europe PubMed Central

PubMed publication ID

8 August 2017

publication date

12 October 2011

1 reference

Europe PubMed Central

PubMed publication ID

8 August 2017

Microbial Cell Factories

1 reference

Europe PubMed Central

PubMed publication ID

8 August 2017

10

1 reference

Europe PubMed Central

PubMed publication ID

8 August 2017

79

1 reference

Europe PubMed Central

PubMed publication ID

8 August 2017

https://scigraph.springernature.com/pub.10.1186/1475-2859-10-79

0 references

Side effects of chaperone gene co-expression in recombinant protein production

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3207889

12 July 2018

Structural Evidence for a Dehydrated Intermediate in Green Fluorescent Protein Chromophore Biosynthesis

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3207889

12 July 2018

Rehosting of bacterial chaperones for high-quality protein production.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3207889

12 July 2018

Microbial factories for recombinant pharmaceuticals

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3207889

12 July 2018

Use of folding modulators to improve heterologous protein production in Escherichia coli.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3207889

12 July 2018

Protein folding and conformational stress in microbial cells producing recombinant proteins: a host comparative overview

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3207889

12 July 2018

Divergent genetic control of protein solubility and conformational quality in Escherichia coli

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3207889

12 July 2018

GroEL plays a central role in stress-induced negative regulation of bacterial conjugation by promoting proteolytic degradation of the activator protein TraJ.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3207889

12 July 2018

Chaperone-based procedure to increase yields of soluble recombinant proteins produced in E. coli

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3207889

12 July 2018

Inclusion body anatomy and functioning of chaperone-mediated in vivo inclusion body disassembly during high-level recombinant protein production in Escherichia coli

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3207889

12 July 2018

Molecular chaperones and protein quality control

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3207889

12 July 2018

Protein quality in bacterial inclusion bodies.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3207889

12 July 2018

Novel insights into the mechanism of chaperone-assisted protein disaggregation

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3207889

12 July 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3207889

12 July 2018

Localization of chaperones DnaK and GroEL in bacterial inclusion bodies

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3207889

12 July 2018

Protein drug stability: a formulation challenge

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3207889

12 July 2018

Soluble expression of recombinant proteins 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=3207889

12 July 2018

Advanced genetic strategies for recombinant protein expression in Escherichia coli

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3207889

12 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=3207889

12 July 2018

Unscrambling an egg: protein disaggregation by AAA+ proteins

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3207889

12 July 2018

Construction and deconstruction 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=3207889

12 July 2018

Soluble expression of cloned phage K11 RNA polymerase gene in Escherichia coli at a low temperature.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3207889

12 July 2018

Trigger factor is involved in GroEL-dependent protein degradation in Escherichia coli and promotes binding of GroEL to unfolded proteins

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3207889

12 July 2018

Three-dimensional structure of beta-galactosidase from E. coli

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3207889

12 July 2018

Truncated GroEL monomer has the ability to promote folding of rhodanese without GroES and ATP.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3207889

12 July 2018

Both the Escherichia coli chaperone systems, GroEL/GroES and DnaK/DnaJ/GrpE, can reactivate heat-treated RNA polymerase. Different mechanisms for the same activity.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3207889

12 July 2018

Cooperation of GroEL/GroES and DnaK/DnaJ heat shock proteins in preventing protein 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=3207889

12 July 2018

Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3207889

12 July 2018

Protocol for preparing proteins with improved solubility by co-expressing with molecular chaperones in Escherichia coli.

1 reference

https://api.crossref.org/works/10.1186%2F1475-2859-10-79

21 January 2018

Learning about protein solubility from bacterial inclusion bodies

1 reference

https://api.crossref.org/works/10.1186%2F1475-2859-10-79

21 January 2018

Role of the chaperone DnaK in protein solubility and conformational quality in inclusion body-forming Escherichia coli cells.

1 reference

https://api.crossref.org/works/10.1186%2F1475-2859-10-79

21 January 2018

Molecular basis for regulation of the heat shock transcription factor sigma32 by the DnaK and DnaJ chaperones.

1 reference

https://api.crossref.org/works/10.1186%2F1475-2859-10-79

21 January 2018

Role of molecular chaperones in inclusion body formation.

1 reference

https://api.crossref.org/works/10.1186%2F1475-2859-10-79

21 January 2018

Substrate shuttling between the DnaK and GroEL systems indicates a chaperone network promoting protein folding.

1 reference

https://api.crossref.org/works/10.1186%2F1475-2859-10-79

21 January 2018

In vivo observation of polypeptide flux through the bacterial chaperonin system.

1 reference

https://api.crossref.org/works/10.1186%2F1475-2859-10-79

21 January 2018

Chaperone protein GrpE and the GroEL/GroES complex promote the correct folding of tobacco mosaic virus coat protein for ribonucleocapsid assembly in vivo

1 reference

https://api.crossref.org/works/10.1186%2F1475-2859-10-79

21 January 2018

GroEL and GroES control of substrate flux in the in vivo folding pathway of phage P22 coat protein.

1 reference

https://api.crossref.org/works/10.1186%2F1475-2859-10-79

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1186%2F1475-2859-10-79

21 January 2018

On the maximum size of proteins to stay and fold in the cavity of GroEL underneath GroES.

1 reference

https://api.crossref.org/works/10.1186%2F1475-2859-10-79

21 January 2018

Yield, solubility and conformational quality of soluble proteins are not simultaneously favored in recombinant Escherichia coli.

1 reference

https://api.crossref.org/works/10.1186%2F1475-2859-10-79

21 January 2018

GroEL/GroES-mediated folding of a protein too large to be encapsulated

1 reference

https://api.crossref.org/works/10.1186%2F1475-2859-10-79

21 January 2018

The impact of dnaKJ overexpression on recombinant protein solubility results from antagonistic effects on the control of protein quality

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3207889

26 September 2018

Rapid degradation of an abnormal protein in Escherichia coli involves the chaperones GroEL and GroES.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3207889

26 September 2018

Rapid protein-folding assay using green fluorescent protein

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3207889

26 September 2018

Optimized release of recombinant proteins by ultrasonication ofE. coli cells

1 reference

https://pubmed.ncbi.nlm.nih.gov/21992454

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Rapid degradation of an abnormal protein in Escherichia coli proceeds through repeated cycles of association with GroEL

1 reference

https://pubmed.ncbi.nlm.nih.gov/21992454

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Recombinant protein solubility—does more mean better?

1 reference

https://pubmed.ncbi.nlm.nih.gov/21992454

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Analytical approaches for assessing aggregation of protein biopharmaceuticals

1 reference

https://pubmed.ncbi.nlm.nih.gov/21992454

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

The position of the heterologous domain can influence the solubility and proteolysis of β-galactosidase fusion proteins in E. coli

1 reference

https://pubmed.ncbi.nlm.nih.gov/21992454

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1186/1475-2859-10-79

1 reference

Europe PubMed Central

PubMed publication ID

8 August 2017

Dimensions Publication ID

0 references

PMC publication ID

1 reference

Europe PubMed Central

PubMed publication ID

8 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

8 August 2017

ResearchGate publication ID

0 references

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