(Q41679938)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9427006%20AND%20SRC:MED&resulttype=core&format=json

8 November 2019

review article

1 reference

title

Structural and mechanistic consequences of polypeptide binding by GroEL (English)

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8 November 2019

5

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8 November 2019

Carol V. Robinson

4

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9427006%20AND%20SRC:MED&resulttype=core&format=json

8 November 2019

author name string

Coyle JE

1

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9427006%20AND%20SRC:MED&resulttype=core&format=json

8 November 2019

Jaeger J

2

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9427006%20AND%20SRC:MED&resulttype=core&format=json

8 November 2019

Gross M

3

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9427006%20AND%20SRC:MED&resulttype=core&format=json

8 November 2019

publication date

1 January 1997

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8 November 2019

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9427006%20AND%20SRC:MED&resulttype=core&format=json

8 November 2019

volume

2

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9427006%20AND%20SRC:MED&resulttype=core&format=json

8 November 2019

page(s)

R93-104

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9427006%20AND%20SRC:MED&resulttype=core&format=json

8 November 2019

issue

6

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9427006%20AND%20SRC:MED&resulttype=core&format=json

GroEL-mediated protein folding

8 November 2019

cites work

1 reference

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7 January 2021

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

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7 January 2021

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

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7 January 2021

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

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7 January 2021

Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL.

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7 January 2021

Mechanism of GroEL action: productive release of polypeptide from a sequestered position under GroES.

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7 January 2021

Molecular chaperones in cellular protein folding

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7 January 2021

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

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7 January 2021

Protein folding in the cell: competing models of chaperonin function.

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7 January 2021

Revisiting the Anfinsen cage

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7 January 2021

A structural model for GroEL-polypeptide recognition

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7 January 2021

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

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7 January 2021

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

1 reference

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7 January 2021

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

1 reference

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7 January 2021

Conformational variability in the refined structure of the chaperonin GroEL at 2.8 A resolution

1 reference

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7 January 2021

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

1 reference

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7 January 2021

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

1 reference

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7 January 2021

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

1 reference

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7 January 2021

Residues in chaperonin GroEL required for polypeptide binding and release

1 reference

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7 January 2021

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

1 reference

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7 January 2021

ATP induces large quaternary rearrangements in a cage-like chaperonin structure.

1 reference

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7 January 2021

The crystal structure of the GroES co-chaperonin at 2.8 Å resolution

1 reference

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7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

The Origins and Consequences of Asymmetry in the Chaperonin Reaction Cycle

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

Chaperone activity and structure of monomeric polypeptide binding domains of GroEL

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

Structural analysis of substrate binding by the molecular chaperone DnaK

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

The antigenic identity of peptide-MHC complexes: a comparison of the conformations of five viral peptides presented by HLA-A2

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

Structural basis of pilus subunit recognition by the PapD chaperone.

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL.

1 reference

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7 January 2021

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

1 reference

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7 January 2021

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

1 reference

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7 January 2021

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

1 reference

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7 January 2021

Chaperonin releases the substrate protein in a form with tendency to aggregate and ability to rebind to chaperonin

1 reference

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7 January 2021

Thermodynamic partitioning model for hydrophobic binding of polypeptides by GroEL. I. GroEL recognizes the signal sequences of beta-lactamase precursor.

1 reference

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7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

The hydrophobic nature of GroEL-substrate binding

1 reference

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7 January 2021

Nature and consequences of GroEL-protein interactions.

1 reference

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7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

Interplay of structure and disorder in cochaperonin mobile loops

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

Model peptide studies demonstrate that amphipathic secondary structures can be recognized by the chaperonin GroEL (cpn60)

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

Folding and activity of hybrid sequence, disulfide-stabilized peptides

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

Complex interactions between the chaperonin 60 molecular chaperone and dihydrofolate reductase

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

Significant hydrogen exchange protection in GroEL-bound DHFR is maintained during iterative rounds of substrate cycling

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

Native-like structure of a protein-folding intermediate bound to the chaperonin GroEL.

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

Structural characterization of the disulfide folding intermediates of bovine alpha-lactalbumin

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

A reexamination of the folding mechanism of dihydrofolate reductase from Escherichia coli: verification and refinement of a four-channel model.

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

Relationship between equilibrium amide proton exchange behavior and the folding pathway of barnase.

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

Local breathing and global unfolding in hydrogen exchange of barnase and its relationship to protein folding pathways

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

Refolding of barnase in the presence of GroE

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

Binding of a chaperonin to the folding intermediates of lactate dehydrogenase

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

Characterization of a quaternary-structured folding intermediate of an antibody Fab-fragment

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

Association of antibody chains at different stages of folding: prolyl isomerization occurs after formation of quaternary structure

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

Importance of electrostatic interactions in the rapid binding of polypeptides to GroEL

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

Peptide Binding by Chaperone SecB: Implications for Recognition of Nonnative Structure

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

Binding affinity of proteins to hsp90 correlates with both hydrophobicity and positive charges. A surface plasmon resonance study

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

Prevention of protein denaturation under heat stress by the chaperonin Hsp60

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

A DNA fragment containing the groE genes can suppress mutations in the Escherichia coli dnaA gene

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

Suppression of the Escherichia coli dnaA46 mutation by amplification of the groES and groEL genes

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

Conformational states bound by the molecular chaperones GroEL and secB: a hidden unfolding (annealing) activity

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

A thermodynamic coupling mechanism for GroEL-mediated unfolding

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

GroEL-mediated folding of structurally homologous dihydrofolate reductases.

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

Detection and characterization of a folding intermediate in barnase by NMR

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

Refolding of Escherichia coli dihydrofolate reductase: sequential formation of substrate binding sites

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

The molecular chaperonin cpn60 displays local flexibility that is reduced after binding with an unfolded protein

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

Structural basis for the binding of proline-rich peptides to SH3 domains

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

Crystal structures of peptide complexes of the amino-terminal SH2 domain of the Syp tyrosine phosphatase

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

The structural basis of sequence-independent peptide binding by OppA protein

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

Characterization of a functionally important mobile domain of GroES.

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

VISTAS: a package for VIsualizing STructures and sequences of proteins

1 reference

https://api.crossref.org/works/10.1016%2FS1359-0278%2897%2900046-1

7 January 2021

10.1016/S1359-0278(97)00046-1

Identifiers

DOI

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9427006%20AND%20SRC:MED&resulttype=core&format=json

8 November 2019

1 reference