(Q36281862)

English

Chaperonin-assisted folding of glutamine synthetase under nonpermissive conditions: off-pathway aggregation propensity does not determine the co-chaperonin requirement

scientific article

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scholarly article

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

Chaperonin-assisted folding of glutamine synthetase under nonpermissive conditions: off-pathway aggregation propensity does not determine the co-chaperonin requirement (English)

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

author name string

P A Voziyan

1

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

M T Fisher

2

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

publication date

1 December 2000

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

Protein Science

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

9

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

12

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

2405-2412

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

The crystal structure of a GroEL/peptide complex: plasticity as a basis for substrate diversity

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144532

30 September 2017

Osmolyte-driven contraction of a random coil protein

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144532

30 September 2017

2 references

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144532

30 September 2017

https://pubmed.ncbi.nlm.nih.gov/11206062

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144532

30 September 2017

A naturally occurring protective system in urea-rich cells: mechanism of osmolyte protection of proteins against urea denaturation

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144532

30 September 2017

Catalysis of protein folding by symmetric chaperone complexes

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144532

30 September 2017

Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysis.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144532

30 September 2017

Folding in vivo of bacterial cytoplasmic proteins: role of GroEL.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144532

30 September 2017

Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144532

30 September 2017

Generation of a stable folding intermediate which can be rescued by the chaperonins GroEL and GroES.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144532

30 September 2017

Molecular chaperones in cellular protein folding

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144532

30 September 2017

Mechanism of GroEL action: Productive release of polypeptide from a sequestered position under groes

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144532

30 September 2017

Living with water stress: evolution of osmolyte systems

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144532

30 September 2017

The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144532

30 September 2017

Oxidative modification of Escherichia coli glutamine synthetase. Decreases in the thermodynamic stability of protein structure and specific changes in the active site conformation.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144532

30 September 2017

GroEL-mediated protein folding

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144532

30 September 2017

Asymmetry, commitment and inhibition in the GroE ATPase cycle impose alternating functions on the two GroEL rings

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144532

29 June 2018

GroE chaperonin-assisted folding and assembly of dodecameric glutamine synthetase.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144532

29 June 2018

Protein folding in the cytosol: chaperonin-dependent and -independent mechanisms

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144532

29 June 2018

Structural aspects of GroEL function

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144532

29 June 2018

The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144532

29 June 2018

Effect of divalent cations on the molecular structure of the GroEL oligomer.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144532

29 June 2018

The effect of groES on the groEL-dependent assembly of dodecameric glutamine synthetase in the presence of ATP and ADP.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144532

29 June 2018

Regulation of glutamine synthetase. I. Purification and properties of glutamine synthetase from Escherichia coli.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144532

29 June 2018

Variability of the intracellular ionic environment of Escherichia coli. Differences between in vitro and in vivo effects of ion concentrations on protein-DNA interactions and gene expression.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144532

29 June 2018

Novel subunit-subunit interactions in the structure of glutamine synthetase.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144532

29 June 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=2144532

29 June 2018

Promotion of the in vitro renaturation of dodecameric glutamine synthetase from Escherichia coli in the presence of GroEL (chaperonin-60) and ATP.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144532

29 June 2018

GroEL accelerates the refolding of hen lysozyme without changing its folding mechanism.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144532

22 September 2018

Thinking outside the box: new insights into the mechanism of GroEL-mediated protein folding.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144532

22 September 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=2144532

22 September 2018

GroES promotes the T to R transition of the GroEL ring distal to GroES in the GroEL-GroES complex.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144532

22 September 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144532

22 September 2018

GroE modulates kinetic partitioning of folding intermediates between alternative states to maximize the yield of biologically active protein.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144532

22 September 2018

The rates of commitment to renaturation of rhodanese and glutamine synthetase in the presence of the groE chaperonins.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144532

22 September 2018

Correlation between the stability of the GroEL-protein ligand complex and the release mechanism.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144532

22 September 2018

The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144532

22 September 2018

Chaperonins can Catalyse the Reversal of Early Aggregation Steps when a Protein Misfolds

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144532

21 October 2018

Changing the nature of the initial chaperonin capture complex influences the substrate folding efficiency

1 reference

https://pubmed.ncbi.nlm.nih.gov/11206062

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings

1 reference

https://pubmed.ncbi.nlm.nih.gov/11206062

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Basis of Substrate Binding by the Chaperonin GroEL†

1 reference

https://pubmed.ncbi.nlm.nih.gov/11206062

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Refolding a glutamine synthetase truncation mutant in vitro: identifying superior conditions using a combination of chaperonins and osmolytes

1 reference

https://pubmed.ncbi.nlm.nih.gov/11206062

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Multiple forms of glutamine synthetase. Hybrid formation by association of adenylylated and unadenylylated subunits

1 reference

https://pubmed.ncbi.nlm.nih.gov/11206062

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Chaperonins facilitate the in vitro folding of monomeric mitochondrial rhodanese

1 reference

https://pubmed.ncbi.nlm.nih.gov/11206062

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

On the role of groES in the chaperonin-assisted folding reaction. Three case studies

1 reference

https://pubmed.ncbi.nlm.nih.gov/11206062

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

The hydrophobic nature of GroEL-substrate binding

1 reference

https://pubmed.ncbi.nlm.nih.gov/11206062

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Interactions between the GroE chaperonins and rhodanese. Multiple intermediates and release and rebinding

1 reference

https://pubmed.ncbi.nlm.nih.gov/11206062

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

The peptide backbone plays a dominant role in protein stabilization by naturally occurring osmolytes

1 reference

https://pubmed.ncbi.nlm.nih.gov/11206062

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Increased efficiency of GroE-assisted protein folding by manganese ions

1 reference

https://pubmed.ncbi.nlm.nih.gov/11206062

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Allosteric control by ATP of non-folded protein binding to GroEL

1 reference

https://pubmed.ncbi.nlm.nih.gov/11206062

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Protein folding Folding with a two-stroke motor

1 reference

https://pubmed.ncbi.nlm.nih.gov/11206062

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Forcing thermodynamically unfolded proteins to fold

1 reference

https://pubmed.ncbi.nlm.nih.gov/11206062

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Overexpression, purification, and properties of GroES from Escherichia coli

1 reference

https://pubmed.ncbi.nlm.nih.gov/11206062

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1110/PS.9.12.2405

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

ResearchGate publication ID

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