(Q43510201)

English

High hydrostatic pressure can probe the effects of functionally related ligands on the quaternary structures of the chaperonins GroEL and GroES.

scientific article published on 20 November 2000

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scholarly article

1 reference

Europe PubMed Central

24 November 2017

High hydrostatic pressure can probe the effects of functionally related ligands on the quaternary structures of the chaperonins GroEL and GroES. (English)

1 reference

Europe PubMed Central

24 November 2017

author name string

Panda M

1

1 reference

Europe PubMed Central

24 November 2017

Ybarra J

2

1 reference

Europe PubMed Central

24 November 2017

Horowitz PM

3

1 reference

Europe PubMed Central

24 November 2017

language of work or name

0 references

publication date

20 November 2000

1 reference

Europe PubMed Central

24 November 2017

Journal of Biological Chemistry

1 reference

Europe PubMed Central

24 November 2017

276

1 reference

Europe PubMed Central

24 November 2017

9

1 reference

Europe PubMed Central

24 November 2017

6253-6259

1 reference

Europe PubMed Central

24 November 2017

Host participation in bacteriophage lambda head assembly

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009530200

21 January 2018

Pressure-induced dissociation of antigen-antibody complexes.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009530200

21 January 2018

Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009530200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009530200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009530200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009530200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009530200

21 January 2018

GroEL/GroES: structure and function of a two-stroke folding machine

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009530200

21 January 2018

Multivalent binding of nonnative substrate proteins by the chaperonin GroEL.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009530200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009530200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009530200

21 January 2018

Chaperonin-facilitated refolding of ribulosebisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (groEL) are K+ dependent

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009530200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009530200

21 January 2018

Coupling between protein folding and allostery in the GroE chaperonin system

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009530200

21 January 2018

Hydrophobic surfaces that are hidden in chaperonin Cpn60 can be exposed by formation of assembly-competent monomers or by ionic perturbation of the oligomer.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009530200

21 January 2018

Mutation Ala2-->Ser destabilizes intersubunit interactions in the molecular chaperone GroEL.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009530200

21 January 2018

Pressure stability of proteins

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009530200

21 January 2018

High pressure effects on protein structure and function

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009530200

21 January 2018

Proteins under pressure. The influence of high hydrostatic pressure on structure, function and assembly of proteins and protein complexes

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009530200

21 January 2018

Pressure-induced reversible dissociation of enolase.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009530200

21 January 2018

The volume and compressibility changes of lysozyme associated with guanidinium chloride and pressure-assisted unfolding.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009530200

21 January 2018

Pressure-induced unfolding of lysozyme in aqueous guanidinium chloride solution

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009530200

21 January 2018

High pressure fosters protein refolding from aggregates at high concentrations

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009530200

21 January 2018

High hydrostatic pressure induces the dissociation of cpn60 tetradecamers and reveals a plasticity of the monomers.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009530200

21 January 2018

Intermediate states of assembly in the dissociation of gastropod hemocyanin by hydrostatic pressure.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009530200

21 January 2018

The stability and hydrophobicity of cytosolic and mitochondrial malate dehydrogenases and their relation to chaperonin-assisted folding.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009530200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009530200

21 January 2018

GroES in the asymmetric GroEL14-GroES7 complex exchanges via an associative mechanism

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009530200

21 January 2018

Residues in chaperonin GroEL required for polypeptide binding and release

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009530200

21 January 2018

Characterization of a functionally important mobile domain of GroES.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009530200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009530200

21 January 2018

Protein folding Folding with a two-stroke motor

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009530200

21 January 2018

Properties of a mutant of Escherichia coli defective in bacteriophage lambda head formation (groE). I. Initial characterization

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009530200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009530200

21 January 2018

GroE facilitates refolding of citrate synthase by suppressing aggregation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009530200

21 January 2018

The chaperonin GroEL is destabilized by binding of ADP

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009530200

21 January 2018

Nucleotide and Mg2+ induced conformational changes in GroEL can be detected by sulfhydryl labeling

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009530200

21 January 2018

Interaction of 4,4'-dithiodipyridine with Cys(458) triggers disassembly of GroEL

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009530200

21 January 2018

Activation and Reaction Volumes in Solution. 3

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009530200

21 January 2018

Reversible oligomerization and denaturation of the chaperonin GroES

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009530200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009530200

21 January 2018

High hydrostatic pressure can reverse aggregation of protein folding intermediates and facilitate acquisition of native structure

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009530200

21 January 2018

Refolding and reassembly of active chaperonin GroEL after denaturation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M009530200

21 January 2018

Identifiers

10.1074/JBC.M009530200

1 reference

Europe PubMed Central

24 November 2017

1 reference

Europe PubMed Central

24 November 2017

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