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The Molten Globule Concept: 45 Years Later

Biochemistry (Moscow), 2018, Vol.83 (Suppl 1), p.S33-S47

2018

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Study of the "molten globule" intermediate state in protein folding by a hydrophobic fluorescent probe

Biopolymers, 1991-01, Vol.31 (1), p.119-128

1991

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Refolding of scFv mini-antibodies using size-exclusion chromatography via arginine solution layer

Journal of chromatography. B, Analytical technologies in the biomedical and life sciences, 2009-07, Vol.877 (22), p.2045-2051

2009

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Molecular chaperone GroEL/ES: Unfolding and refolding processes

Biochemistry (Moscow), 2013-12, Vol.78 (13), p.1405-1414

2013

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Affinity chromatography of chaperones based on denatured proteins: Analysis of cell lysates of different origin

Protein expression and purification, 2016-03, Vol.119, p.117-123

2016

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Ligand-Induced Reassembly of GroEL/ES Chaperone In Vitro: Visualization by Electron Microscopy

Molecular biology (New York), 2018, Vol.52 (1), p.103-107

2018

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Evidence for a molten globule state as a general intermediate in protein folding

FEBS letters, 1990-03, Vol.262 (1), p.20-24

1990

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Limited Trypsinolysis of GroES: The Effect on the Interaction with GroEL and Assembly In Vitro

Molecular biology (New York), 2018, Vol.52 (1), p.69-74

2018

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‘All-or-none’ mechanism of the molten globule unfolding

FEBS letters, 1992-12, Vol.314 (1), p.89-92

1992

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Temperature-induced conformational transitions of the glucanotransferase Bgl2p isolated from Saccharomyces cerevisiae cell walls

Molecular biology (New York), 2010-06, Vol.44 (3), p.488-491

2010

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Dataset concerning GroEL chaperonin interaction with proteins

Data in brief, 2016-03, Vol.6, p.619-624

2016

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On the role of some conserved and nonconserved amino acid residues in the transitional state and intermediate of apomyoglobin folding

Molecular biology (New York), 2009-02, Vol.43 (1), p.123-133

2009

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GroES co-chaperonin small-angle X-ray scattering study shows ring orifice increase in solution

FEBS letters, 2000-04, Vol.471 (2), p.211-214

2000

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Kinetic refolding of beta-lactoglobulin. Studies by synchrotron X-ray scattering, and circular dichroism, absorption and fluorescence spectroscopy

Journal of molecular biology, 1998-01, Vol.275 (1), p.149-162

1998

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Sequential mechanism of refolding of carbonic anhydrase B

FEBS letters, 1987-11, Vol.224 (1), p.9-13

1987

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Protein Globularization During Folding. A Study by Synchrotron Small-angle X-ray Scattering

Journal of molecular biology, 1996-10, Vol.262 (4), p.559-574

1996

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α-lactalbumin: compact state with fluctuating tertiary structure?

FEBS letters, 1981-12, Vol.136 (2), p.311-315

1981

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Ligands regulate GroEL thermostability

FEBS letters, 1997-04, Vol.405 (3), p.260-262

1997

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Affinity chromatography of GroEL chaperonin based on denatured proteins: role of electrostatic interactions in regulation of GroEL affinity for protein substrates

Biochemistry (Moscow), 2006-12, Vol.71 (12), p.1357-1364

2006

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Ligand-Induced Reassembly of GroEL/ES Chaperone In Vitro: Visualization by Electron Microscopy

Molekuliarnaia biologiia, 2018-01, Vol.52 (1), p.120

2018

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Two slow stages in refolding of bovine carbonic anhydrase B are due to proline isomerization

Journal of molecular biology, 1990-06, Vol.213 (3), p.561-568

1990

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Homogeneous assay for biotin based on Aequorea victoria bioluminescence resonance energy transfer system

Analytical biochemistry, 2003-02, Vol.313 (1), p.68-75

2003

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Limited Trypsinolysis of GroES: The Effect on the Interaction with GroEL and Assembly In Vitro

Molekuliarnaia biologiia, 2018-01, Vol.52 (1), p.82

2018

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Compact state of a protein molecule with pronounced small-scale mobility: bovine alpha-lactalbumin

European biophysics journal, 1985-01, Vol.13 (2), p.109-121

1985

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Folding/Unfolding Kinetics of Apomyoglobin

Molecular biology (New York), 2005-11, Vol.39 (6), p.884-891

2005

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The Molten Globule Concept: 45 Years Later

Study of the "molten globule" intermediate state in protein folding by a hydrophobic fluorescent probe

Refolding of scFv mini-antibodies using size-exclusion chromatography via arginine solution layer

Molecular chaperone GroEL/ES: Unfolding and refolding processes

Affinity chromatography of chaperones based on denatured proteins: Analysis of cell lysates of different origin

Ligand-Induced Reassembly of GroEL/ES Chaperone In Vitro: Visualization by Electron Microscopy

Evidence for a molten globule state as a general intermediate in protein folding

Limited Trypsinolysis of GroES: The Effect on the Interaction with GroEL and Assembly In Vitro

‘All-or-none’ mechanism of the molten globule unfolding

Temperature-induced conformational transitions of the glucanotransferase Bgl2p isolated from Saccharomyces cerevisiae cell walls

Dataset concerning GroEL chaperonin interaction with proteins

On the role of some conserved and nonconserved amino acid residues in the transitional state and intermediate of apomyoglobin folding

GroES co-chaperonin small-angle X-ray scattering study shows ring orifice increase in solution

Kinetic refolding of beta-lactoglobulin. Studies by synchrotron X-ray scattering, and circular dichroism, absorption and fluorescence spectroscopy

Sequential mechanism of refolding of carbonic anhydrase B

Protein Globularization During Folding. A Study by Synchrotron Small-angle X-ray Scattering

α-lactalbumin: compact state with fluctuating tertiary structure?

Ligands regulate GroEL thermostability

Affinity chromatography of GroEL chaperonin based on denatured proteins: role of electrostatic interactions in regulation of GroEL affinity for protein substrates

Ligand-Induced Reassembly of GroEL/ES Chaperone In Vitro: Visualization by Electron Microscopy

Two slow stages in refolding of bovine carbonic anhydrase B are due to proline isomerization

Homogeneous assay for biotin based on Aequorea victoria bioluminescence resonance energy transfer system

Limited Trypsinolysis of GroES: The Effect on the Interaction with GroEL and Assembly In Vitro

Compact state of a protein molecule with pronounced small-scale mobility: bovine alpha-lactalbumin

Folding/Unfolding Kinetics of Apomyoglobin

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