(Q31446965)

2 July 2017

title

Excluded volume effects on the refolding and assembly of an oligomeric protein. GroEL, a case study (English)

1 reference

2 July 2017

1 reference

Galan A

1

1 reference

2 July 2017

Sot B

2

1 reference

2 July 2017

Llorca O

3

1 reference

2 July 2017

Carrascosa JL

4

1 reference

2 July 2017

Valpuesta JM

5

1 reference

2 July 2017

Muga A

6

1 reference

2 July 2017

publication date

1 January 2001

1 reference

Journal of Biological Chemistry

2 July 2017

language of work or name

English

0 references

published in

1 reference

2 July 2017

volume

276

1 reference

2 July 2017

issue

2

1 reference

2 July 2017

page(s)

957-964

1 reference

Molecular chaperone functions of heat-shock proteins

2 July 2017

cites work

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M006861200

GroEL-mediated protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M006861200

Residues in chaperonin GroEL required for polypeptide binding and release

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M006861200

The formation of symmetrical GroEL-GroES complexes in the presence of ATP.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M006861200

A Monomeric Variant of GroEL Binds Nucleotides but Is Inactive as a Molecular Chaperone

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M006861200

(Mg-ATP)-dependent self-assembly of molecular chaperone GroEL.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M006861200

A carboxy-terminal deletion impairs the assembly of GroEL and confers a pleiotropic phenotype in Escherichia coli K-12.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M006861200

Stabilization of a compact conformation of monomeric GroEL at low temperature by adenine nucleotides

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M006861200

Macromolecular crowding: biochemical, biophysical, and physiological consequences

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M006861200

Influence of excluded volume upon macromolecular structure and associations in 'crowded' media

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M006861200

Confinement as a determinant of macromolecular structure and reactivity.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M006861200

Implications of macromolecular crowding for protein assembly.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M006861200

Release of both native and non-native proteins from a cis-only GroEL ternary complex

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M006861200

The effect of macromolecular crowding on chaperonin-mediated protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M006861200

Effects of macromolecular crowding on protein folding and aggregation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M006861200

Nonspecific stabilization of stress-susceptible proteins by stress-resistant proteins: a model for the biological role of heat shock proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M006861200

Physical Mapping of the Mouse Genome

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M006861200

A kinetic study of the competition between renaturation and aggregation during the refolding of denatured-reduced egg white lysozyme

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M006861200

9 Escherichia coli phage T4 topoisomerase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M006861200

Structure and thermal denaturation of crystalline and noncrystalline cytochrome oxidase as studied by infrared spectroscopy

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M006861200

Conformational changes in the GroEL oligomer during the functional cycle

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M006861200

Determination of protein secondary structure by Fourier transform infrared spectroscopy: a critical assessment

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M006861200

Ligands regulate GroEL thermostability

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M006861200

Hydrolysis of adenosine 5'-triphosphate by Escherichia coli GroEL: effects of GroES and potassium ion.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M006861200

Hindered diffusion of inert tracer particles in the cytoplasm of mouse 3T3 cells

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M006861200

The mitochondrial chaperonin hsp60 is required for its own assembly

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M006861200

In Vivo Observation of Polypeptide Flux through the Bacterial Chaperonin System

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M006861200

Isolation and biochemical characterization of highly purified Escherichia coli molecular chaperone Cpn60 (GroEL) by affinity chromatography and urea-induced monomerization

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M006861200

Estimation of macromolecule concentrations and excluded volume effects for the cytoplasm of Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M006861200

Physical properties of cytoplasm

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M006861200

Folding and binding cascades: dynamic landscapes and population shifts

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M006861200

Molecular chaperones: Avoiding the crowd

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M006861200

Excluded volume as a determinant of macromolecular structure and reactivity

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M006861200

The oligomeric structure of GroEL/GroES is required for biologically significant chaperonin function in protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M006861200

21 January 2018

GroEL under Heat-Shock

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M006861200

Effects of the Inter-ring Communication in GroEL Structural and Functional Asymmetry

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M006861200

ATP hydrolysis induces an intermediate conformational state in GroEL

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M006861200

Tetradecameric chaperonin 60 can be assembled in vitro from monomers in a process that is ATP independent

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M006861200

Refolding and Reassembly of Active Chaperonin GroEL After Denaturation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M006861200

Ribonuclease A Revisited: Infrared Spectroscopic Evidence for Lack of Native-like Secondary Structures in the Thermally Denatured State

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M006861200

Apocytochrome c interaction with phospholipid membranes studied by Fourier-transform infrared spectroscopy

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M006861200

Thermodynamic stability and folding of GroEL minichaperones

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M006861200

Unfolding and disassembly of the chaperonin GroEL occurs via a tetradecameric intermediate with a folded equatorial domain

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M006861200

Effects of dextran on the self-association of human spectrin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M006861200

Direct observation of the self-association of dilute proteins in the presence of inert macromolecules at high concentration via tracer sedimentation equilibrium: theory, experiment, and biological significance

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M006861200

Protein folding: Thickening the broth

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M006861200

21 January 2018

Identifiers

DOI

10.1074/JBC.M006861200

1 reference

2 July 2017

1 reference