Molecular chaperones and their interactions investigated by analytical ultracentrifugation and other methodologies (Q74420389)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9534169%20AND%20SRC:MED&resulttype=core&format=json

10 November 2019

title

Molecular chaperones and their interactions investigated by analytical ultracentrifugation and other methodologies (English)

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10 November 2019

author name string

H J Schönfeld

series ordinal

1

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10 November 2019

J Behlke

series ordinal

2

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10 November 2019

publication date

1 January 1998

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10 November 2019

published in

Methods in Enzymology

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10 November 2019

volume

290

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10 November 2019

page(s)

269-296

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DnaK ATPase activity revisited

10 November 2019

cites work

1 reference

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7 January 2021

The DnaK chaperone system of Escherichia coli: quaternary structures and interactions of the DnaK and GrpE components.

1 reference

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7 January 2021

Self-Association of the Molecular Chaperone HSC70

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7 January 2021

Physical interactions between members of the DnaK chaperone machinery: characterization of the DnaK.GrpE complex

1 reference

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7 January 2021

Purification and properties of groE, a host protein involved in bacteriophage assembly

1 reference

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7 January 2021

Divergent effects of ATP on the binding of the DnaK and DnaJ chaperones to each other, or to their various native and denatured protein substrates.

1 reference

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7 January 2021

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

1 reference

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7 January 2021

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

1 reference

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7 January 2021

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

1 reference

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7 January 2021

Fluorescence detection of symmetric GroEL14(GroES7)2 heterooligomers involved in protein release during the chaperonin cycle

1 reference

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7 January 2021

Analytical ultracentrifugation reborn

1 reference

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7 January 2021

Analytical ultracentrifugation of complex macromolecular systems

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7 January 2021

Molecular mass determination by sedimentation velocity experiments and direct fitting of the concentration profiles

1 reference

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7 January 2021

Conformational characterization of DnaK and its complexes by small-angle X-ray scattering

1 reference

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7 January 2021

Osmotic pressure measurements, of the ligand-linked dissociation equilibrium of human oxyhemoglobin

1 reference

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7 January 2021

Potassium ions and the molecular-chaperone activity of DnaK.

1 reference

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7 January 2021

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

1 reference

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7 January 2021

Structure-function analysis of the zinc finger region of the DnaJ molecular chaperone

1 reference

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7 January 2021

A novel function of Escherichia coli chaperone DnaJ. Protein-disulfide isomerase.

1 reference

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7 January 2021

Overexpression in Escherichia coli, purification and characterization of the molecular chaperone HSC70.

1 reference

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7 January 2021

Effect of nucleotides, peptides, and unfolded proteins on the self-association of the molecular chaperone HSC70

1 reference

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7 January 2021

A novel factor required for the assembly of the DnaK and DnaJ chaperones of Thermus thermophilus

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2898%2990025-8

7 January 2021

Polymerization of 70-kDa heat shock protein by yeast DnaJ in ATP

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2898%2990025-8

7 January 2021

ATP-induced protein-Hsp70 complex dissociation requires K+ but not ATP hydrolysis.

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2898%2990025-8

7 January 2021

Nucleotide-induced conformational changes in the ATPase and substrate binding domains of the DnaK chaperone provide evidence for interdomain communication

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2898%2990025-8

7 January 2021

Effect of constitutive 70-kDa heat shock protein polymerization on its interaction with protein substrate

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2898%2990025-8

7 January 2021

Structural analysis of substrate binding by the molecular chaperone DnaK

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2898%2990025-8

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%2FS0076-6879%2898%2990025-8

7 January 2021

Biochemical Characterization of Symmetric GroEL-GroES Complexes

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2898%2990025-8

7 January 2021

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2898%2990025-8

7 January 2021

Residues in chaperonin GroEL required for polypeptide binding and release

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2898%2990025-8

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2898%2990025-8

7 January 2021

Identification of nucleotide-binding regions in the chaperonin proteins GroEL and GroES.

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2898%2990025-8

7 January 2021

GroES and the chaperonin-assisted protein folding cycle: GroES has no affinity for nucleotides

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2898%2990025-8

7 January 2021

Nucleotide-dependent complex formation between the Escherichia coli chaperonins GroEL and GroES studied under equilibrium conditions.

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2898%2990025-8

7 January 2021

Monomer-heptamer equilibrium of the Escherichia coli chaperonin GroES.

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2898%2990025-8

7 January 2021

The C-terminal sequence of the chaperonin GroES is required for oligomerization

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2898%2990025-8

7 January 2021

Reversible oligomerization and denaturation of the chaperonin GroES

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2898%2990025-8

7 January 2021

The chaperonin GroEL is destabilized by binding of ADP

1 reference

https://api.crossref.org/works/10.1016%2FS0076-6879%2898%2990025-8

7 January 2021

10.1016/S0076-6879(98)90025-8

Identifiers

DOI

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9534169%20AND%20SRC:MED&resulttype=core&format=json

10 November 2019

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