How GroES regulates binding of nonnative protein to GroEL. (Q54565510)

1 June 2018

title

How GroES regulates binding of nonnative protein to GroEL. (English)

1 reference

1 June 2018

author name string

Sparrer H

series ordinal

1

1 reference

1 June 2018

Buchner J

series ordinal

2

1 reference

1 June 2018

language of work or name

English

0 references

publication date

1 May 1997

1 reference

1 June 2018

Journal of Biological Chemistry

number of pages

7

1 reference

based on heuristic

inferred from page(s)

published in

1 reference

1 June 2018

volume

272

1 reference

1 June 2018

issue

22

1 reference

1 June 2018

page(s)

14080-14086

1 reference

1 June 2018

Molecular chaperones in cellular protein folding

cites work

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.22.14080

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.22.14080

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.22.14080

Residues in chaperonin GroEL required for polypeptide binding and release

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.22.14080

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.22.14080

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.22.14080

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.22.14080

Nucleotide binding-promoted conformational changes release a nonnative polypeptide from the Escherichia coli chaperonin GroEL.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.22.14080

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.22.14080

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.22.14080

The Origins and Consequences of Asymmetry in the Chaperonin Reaction Cycle

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.22.14080

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.22.14080

High selectivity with low specificity: how SecB has solved the paradox of chaperone binding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.22.14080

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.22.14080

Analysis of numerical methods for computer simulation of kinetic processes: development of KINSIM--a flexible, portable system.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.22.14080

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.22.14080

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.22.14080

Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.22.14080

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.22.14080

Catalysis of protein folding by symmetric chaperone complexes

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.22.14080

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.272.22.14080

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.22.14080

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.22.14080

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.22.14080

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.22.14080

21 January 2018

Identifiers

DOI

10.1074/JBC.272.22.14080

1 reference

1 June 2018

1 reference

1 June 2018