(Q33431560)

26 July 2017

title

Activation parameters for the spontaneous and pressure-induced phases of the dissociation of single-ring GroEL (SR1) chaperonin (English)

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26 July 2017

Markandeswar Panda

1

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26 July 2017

Paul M Horowitz

series ordinal

2

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26 July 2017

language of work or name

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1 January 2004

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26 July 2017

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26 July 2017

volume

23

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26 July 2017

issue

1

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26 July 2017

page(s)

85-94

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Dissociation of the single-ring chaperonin GroEL by high hydrostatic pressure

26 July 2017

cites work

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12 December 2020

Pressure stability of proteins

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12 December 2020

Compressibility of protein transitions

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12 December 2020

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

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12 December 2020

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

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12 December 2020

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

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12 December 2020

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

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12 December 2020

Close identity of a pressure-stabilized intermediate with a kinetic intermediate in protein folding

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12 December 2020

Chaperonin-mediated protein folding

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12 December 2020

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

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12 December 2020

Review: a structural view of the GroE chaperone cycle

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12 December 2020

The chaperonin GroEL is destabilized by binding of ADP

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12 December 2020

Deterministic pressure dissociation and unfolding of triose phosphate isomerase: persistent heterogeneity of a protein dimer

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12 December 2020

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

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12 December 2020

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

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12 December 2020

Partial molar volume, surface area, and hydration changes for equilibrium unfolding and formation of aggregation transition state: high-pressure and cosolute studies on recombinant human IFN-gamma

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12 December 2020

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

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12 December 2020

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

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12 December 2020

Structural basis for GroEL-assisted protein folding from the crystal structure of (GroEL-KMgATP)14 at 2.0A resolution

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12 December 2020

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

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12 December 2020

Investigation of the effect of high hydrostatic pressure on proteins and lipidic membranes by dynamic fluorescence spectroscopy

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12 December 2020

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

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12 December 2020

High pressure effects on protein structure and function

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12 December 2020

GroE facilitates refolding of citrate synthase by suppressing aggregation

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12 December 2020

The Escherichia coli heat shock proteins GroEL and GroES modulate the folding of the beta-lactamase precursor

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12 December 2020

Protein folding Folding with a two-stroke motor

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12 December 2020

From minichaperone to GroEL 3: properties of an active single-ring mutant of GroEL.

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12 December 2020

Cooperative effects of potassium, magnesium, and magnesium-ADP on the release of Escherichia coli dihydrofolate reductase from the chaperonin GroEL.

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12 December 2020

Fluorescence and FTIR study of pressure-induced structural modifications of horse liver alcohol dehydrogenase (HLADH).

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12 December 2020

Protein folding as a diffusional process

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12 December 2020

Pressure-induced reversible dissociation of enolase.

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12 December 2020

The pressure-temperature free energy-landscape of staphylococcal nuclease monitored by (1)H NMR.

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12 December 2020

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

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12 December 2020

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

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12 December 2020

High-pressure 1H NMR study of pressure-induced structural changes in the heme environments of metcyanomyoglobins

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12 December 2020

Tobacco mosaic virus disassembly by high hydrostatic pressure in combination with urea and low temperature

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12 December 2020

GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings

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12 December 2020

Pressure effects on the structure of oligomeric proteins prior to subunit dissociation.

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12 December 2020

High pressure effects on biological macromolecules: from structural changes to alteration of cellular processes

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12 December 2020

Construction of single-ring and two-ring hybrid versions of bacterial chaperonin GroEL

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12 December 2020

Alternative prion structural changes revealed by high pressure.

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12 December 2020

Pressure provides new insights into protein folding, dynamics and structure

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12 December 2020

Volume, expansivity and isothermal compressibility changes associated with temperature and pressure unfolding of staphylococcal nuclease 1 1Edited by C. R. Mathews

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12 December 2020

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

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12 December 2020

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

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12 December 2020

Pressure denaturation of proteins: evaluation of compressibility effects

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12 December 2020

High pressure effects on proteins and other biomolecules

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12 December 2020

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

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12 December 2020

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

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12 December 2020

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

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12 December 2020

Revisiting volume changes in pressure-induced protein unfolding.

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12 December 2020

Activation and Reaction Volumes in Solution. 3

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12 December 2020

The crystal structure of the bacterial chaperonin GroEL at 2.8 A

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12 December 2020

High pressure fosters protein refolding from aggregates at high concentrations

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12 December 2020

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

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12 December 2020

Conformational heterogeneity is revealed in the dissociation of the oligomeric chaperonin GroEL by high hydrostatic pressure.

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12 December 2020

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

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12 December 2020

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

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12 December 2020

10.1023/B:JOPC.0000016262.27420.3A

Identifiers

DOI

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Dimensions Publication ID

26 July 2017

1048995869

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