(Q41429098)

30 September 2017

1 reference

title

GroEL-mediated protein folding (English)

1 reference

30 September 2017

0 references

Fenton WA

1

1 reference

PMCID

2144759

30 September 2017

Horwich AL

series ordinal

2

1 reference

30 September 2017

1 April 1997

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30 September 2017

1 reference

30 September 2017

6

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30 September 2017

743-760

1 reference

30 September 2017

4

1 reference

beta-Lactamase binds to GroEL in a conformation highly protected against hydrogen/deuterium exchange

30 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

A thermodynamic coupling mechanism for GroEL-mediated unfolding

1 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

GroEL binds to and unfolds rhodanese posttranslationally

1 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

Toward a mechanism for GroEL.GroES chaperone activity: an ATPase-gated and -pulsed folding and annealing cage

1 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains.

1 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

Chaperonin-facilitated protein folding: optimization of rate and yield by an iterative annealing mechanism

1 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

The protein-folding activity of chaperonins correlates with the symmetric GroEL14(GroES7)2 heterooligomer

1 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

Protein folding in the central cavity of the GroEL-GroES chaperonin complex

1 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

Structure of the heat shock protein chaperonin-10 of Mycobacterium leprae

1 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

Early events in preprotein recognition in E. coli: interaction of SRP and trigger factor with nascent polypeptides.

1 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

Specificity of DnaK-peptide binding

1 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

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

1 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

A polypeptide bound by the chaperonin groEL is localized within a central cavity

1 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

Statistical mechanics of kinetic proofreading in protein folding in vivo

1 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

1 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

Conformational specificity of the chaperonin GroEL for the compact folding intermediates of alpha-lactalbumin

1 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

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

1 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

Folding intermediate binds to the bottom of bullet-shaped holo-chaperonin and is readily accessible to antibody.

1 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP.

1 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage.

1 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

The folding of GroEL-bound barnase as a model for chaperonin-mediated protein folding

1 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

Interaction of GroEL with a highly structured folding intermediate: iterative binding cycles do not involve unfolding

1 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

Principles that govern the folding of protein chains

1 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

Escherichia coli dnaK null mutants are inviable at high temperature

1 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

Cellular defects caused by deletion of the Escherichia coli dnaK gene indicate roles for heat shock protein in normal metabolism

1 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

The Escherichia coli heat shock proteins GroEL and GroES modulate the folding of the beta-lactamase precursor

1 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate

1 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

The translation machinery and 70 kd heat shock protein cooperate in protein synthesis

1 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

Prevention of protein denaturation under heat stress by the chaperonin Hsp60

1 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

Cooperation of GroEL/GroES and DnaK/DnaJ heat shock proteins in preventing protein misfolding in Escherichia coli

1 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

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

1 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy.

11 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

Amino acid specificity of the Escherichia coli chaperone GroEL (heat shock protein 60).

11 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

Reversal by GroES of the GroEL preference from hydrophobic amino acids toward hydrophilic amino acids.

11 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

The chaperonin GroEL does not recognize apo-alpha-lactalbumin in the molten globule state.

11 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

Purification and properties of the groES morphogenetic protein of Escherichia coli

11 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

Demonstration by genetic suppression of interaction of GroE products with many proteins.

11 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

Interaction of Hsp 70 with newly synthesized proteins: implications for protein folding and assembly.

11 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

Reconstitution of a heat shock effect in vitro: influence of GroE on the thermal aggregation of .alpha.-glucosidase from yeast

11 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

The chaperonin GroEL binds a polypeptide in an .alpha.-helical conformation

11 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

GroE prevents the accumulation of early folding intermediates of pre-beta-lactamase without changing the folding pathway.

11 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

Theory of chaperonin action: inertial model for enhancement of prokaryotic Rubisco assembly

11 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

Purified chaperonin 60 (groEL) interacts with the nonnative states of a multitude of Escherichia coli proteins

11 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

Chaperonin-mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity

11 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

Interaction of GroE with an all-beta-protein

11 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

Positive cooperativity in the functioning of molecular chaperone GroEL

11 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

Different conformations for the same polypeptide bound to chaperones DnaK and GroEL.

11 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

Solution structures of GroEL and its complex with rhodanese from small-angle neutron scattering.

11 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

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

19 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

Determination of regions in the dihydrofolate reductase structure that interact with the molecular chaperonin GroEL.

19 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

Dynamics of the GroEL-protein complex: effects of nucleotides and folding mutants.

19 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

Characterization of a functionally important mobile domain of GroES.

19 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: implications for the mechanism of assisted protein folding.

19 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

Does compactness induce secondary structure in proteins? A study of poly-alanine chains computed by distance geometry

19 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

Different peptide binding specificities of hsp70 family members.

19 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

Conformation of GroEL-bound alpha-lactalbumin probed by mass spectrometry.

19 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

Two lines of allosteric communication in the oligomeric chaperonin GroEL are revealed by the single mutation Arg196-->Ala.

19 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

Selective in vivo rescue by GroEL/ES of thermolabile folding intermediates to phage P22 structural proteins.

19 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

Thermodynamic partitioning model for hydrophobic binding of polypeptides by GroEL. II. GroEL recognizes thermally unfolded mature beta-lactamase.

19 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

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

19 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

Destabilization of the complete protein secondary structure on binding to the chaperone GroEL.

19 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

Kinetic analysis of interactions between GroEL and reduced alpha-lactalbumin. Effect of GroES and nucleotides.

19 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

Asymmetrical interaction of GroEL and GroES in the ATPase cycle of assisted protein folding.

19 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

Functional significance of symmetrical versus asymmetrical GroEL-GroES chaperonin complexes.

19 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

Nature and consequences of GroEL-protein interactions.

19 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

BiP binding sequences in antibodies.

19 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

The Origins and Consequences of Asymmetry in the Chaperonin Reaction Cycle

19 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

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

2 December 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144759

Binding of defined regions of a polypeptide to GroEL and its implications for chaperonin-mediated protein folding

2 December 2018

1 reference

12 December 2020

Peptide binding and release by proteins implicated as catalysts of protein assembly

1 reference

12 December 2020

Chaperonins facilitate the in vitro folding of monomeric mitochondrial rhodanese

1 reference

12 December 2020

Specificity in chaperonin-mediated protein folding

1 reference

12 December 2020

Stability of wild-type and temperature-sensitive protein subunits of the phage P22 capsid

1 reference

12 December 2020

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

1 reference

12 December 2020

Increased efficiency of GroE-assisted protein folding by manganese ions

1 reference

12 December 2020

Complex interactions between the chaperonin 60 molecular chaperone and dihydrofolate reductase

1 reference

12 December 2020

Cooperativity in ATP hydrolysis by GroEL is increased by GroES

1 reference

12 December 2020

A newly synthesized protein interacts with GroES on the surface of chaperonin GroEL

1 reference

12 December 2020

Interactions of phage P22 tailspike protein with GroE molecular chaperones during refolding in vitro

1 reference

12 December 2020

Refolding of barnase in the presence of GroE

1 reference

12 December 2020

Characterization of a functional GroEL14(GroES7)2 chaperonin hetero-oligomer

1 reference

12 December 2020

Symmetric complexes of GroE chaperonins as part of the functional cycle

1 reference

12 December 2020

GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms

1 reference

12 December 2020

The hydrophobic nature of GroEL-substrate binding

1 reference

12 December 2020

Homologous proteins with different affinities for groEL. The refolding of the aspartate aminotransferase isozymes at varying temperatures

1 reference

12 December 2020

Biochemical Characterization of Symmetric GroEL-GroES Complexes

1 reference

12 December 2020

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

1 reference

12 December 2020

The 2.4 A crystal structure of the bacterial chaperonin GroEL complexed with ATP gamma S

1 reference

12 December 2020

Catalysis of amide proton exchange by the molecular chaperones GroEL and SecB

1 reference

12 December 2020

Effect of single point mutations in citrate synthase on binding to GroEL

1 reference

12 December 2020

Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction

1 reference

12 December 2020

Effect of GroEL on the re-folding kinetics of alpha-lactalbumin

1 reference

12 December 2020

Identifiers

DOI

10.1002/PRO.5560060401

1 reference

30 September 2017

1 reference

30 September 2017

1 reference

PMCID

2144759