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Hydrophobic plant antioxidants. Preparation of nanoparticles and their application for prevention of neurodegenerative diseases. Review and experimental data

Current topics in medicinal chemistry, 2014-01, Vol.14 (22), p.2520

2014

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Mechanism of Thermal Aggregation of Rabbit Muscle Glyceraldehyde-3-phosphate Dehydrogenase

Biochemistry (Easton), 2006-11, Vol.45 (44), p.13375-13384

2006

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A protein aggregation based test for screening of the agents affecting thermostability of proteins

PloS one, 2011-07, Vol.6 (7), p.e22154-e22154

2011

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Kinetics of aggregation of UV-irradiated glyceraldehyde-3-phosphate dehydrogenase from rabbit skeletal muscle. Effect of agents possessing chaperone-like activity

Biophysical chemistry, 2012-04, Vol.163-164, p.11-20

2012

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Evidence for the formation of start aggregates as an initial stage of protein aggregation

FEBS letters, 2007-09, Vol.581 (22), p.4223-4227

2007

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Effect of 2-hydroxypropyl-β-cyclodextrin on thermal inactivation, denaturation and aggregation of glyceraldehyde-3-phosphate dehydrogenase from rabbit skeletal muscle

International journal of biological macromolecules, 2010-06, Vol.46 (5), p.487-492

2010

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Effect of α-crystallin on thermal denaturation and aggregation of rabbit muscle glyceraldehyde-3-phosphate dehydrogenase

Biophysical chemistry, 2007-02, Vol.125 (2), p.521-531

2007

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Misfolded forms of glyceraldehyde‐3‐phosphate dehydrogenase interact with GroEL and inhibit chaperonin‐assisted folding of the wild‐type enzyme

Protein science, 2005-04, Vol.14 (4), p.921-928

2005

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Comparative Analysis of the Effects of α-Crystallin and GroEL on the Kinetics of Thermal Aggregation of Rabbit Muscle Glyceraldehyde-3-Phosphate Dehydrogenase

The Protein Journal, 2010, Vol.29 (1), p.11-25

2010

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Interaction of Polyanions with Basic Proteins, 2

Macromolecular bioscience, 2005-12, Vol.5 (12), p.1184-1192

2005

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Participation of chaperonin GroEL in the folding of D-glyceraldehyde-3-phosphate dehydrogenase. An approach based on the use of different oligomeric forms of the enzyme immobilized on sepharose

Journal of Protein Chemistry, 1999-01, Vol.18 (1), p.79-87

1999

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Comparative Analysis of the Effects of [alpha]-Crystallin and GroEL on the Kinetics of Thermal Aggregation of Rabbit Muscle Glyceraldehyde-3-Phosphate Dehydrogenase

The Protein Journal, 2010-01, Vol.29 (1), p.11

2010

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Interaction of polyanions with basic proteins, 2(a) : influence of complexing polyanions on the thermo-aggregation of oligomeric enzymes

Macromolecular bioscience, 2005-12, Vol.5 (12), p.1184-1192

2005

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Interaction of polyanions with basic proteins, 2a Influence of complexing polyanions on the thermoaggregation of oligomeric enzymes

Macromolecular bioscience, 2005, Vol.5 (12), p.1184-1192

2005

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SH-containing compounds as allosteric effectors of glyceraldehyde-3-phosphate dehydrogenase

FEBS letters, 1993-12, Vol.336 (2), p.208-210

1993

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D-glyceraldehyde-3-phosphate dehydrogenase. Properties of the enzyme modified at arginine residues

Applied biochemistry and biotechnology, 1996-10, Vol.61 (1-2), p.47-56

1996

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Thermal unfolding of phosphorylating d-glyceraldehyde-3-phosphate dehydrogenase studied by differential scanning calorimetry

Biochimica et biophysica acta, 1999-08, Vol.1433 (1), p.294-306

1999

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Rabbit muscle D-Glyceraldehyde-3-phosphate dehydrogenase: Half-of-the-sites reactivity of the enzyme modified at arginine residues

Biochemical and biophysical research communications, 1992-09, Vol.187 (2), p.577-583

1992

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Auramine O as a Conformational Probe to Study Glyceraldehyde 3‐Phosphate Dehydrogenase

European journal of biochemistry, 1982-07, Vol.125 (2), p.291-297

1982

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Hydrophobic plant antioxidants. Preparation of nanoparticles and their application for prevention of neurodegenerative diseases. Review and experimental data

Mechanism of Thermal Aggregation of Rabbit Muscle Glyceraldehyde-3-phosphate Dehydrogenase

A protein aggregation based test for screening of the agents affecting thermostability of proteins

Kinetics of aggregation of UV-irradiated glyceraldehyde-3-phosphate dehydrogenase from rabbit skeletal muscle. Effect of agents possessing chaperone-like activity

Evidence for the formation of start aggregates as an initial stage of protein aggregation

Effect of 2-hydroxypropyl-β-cyclodextrin on thermal inactivation, denaturation and aggregation of glyceraldehyde-3-phosphate dehydrogenase from rabbit skeletal muscle

Effect of α-crystallin on thermal denaturation and aggregation of rabbit muscle glyceraldehyde-3-phosphate dehydrogenase

Misfolded forms of glyceraldehyde‐3‐phosphate dehydrogenase interact with GroEL and inhibit chaperonin‐assisted folding of the wild‐type enzyme

Comparative Analysis of the Effects of α-Crystallin and GroEL on the Kinetics of Thermal Aggregation of Rabbit Muscle Glyceraldehyde-3-Phosphate Dehydrogenase

Interaction of Polyanions with Basic Proteins, 2

Participation of chaperonin GroEL in the folding of D-glyceraldehyde-3-phosphate dehydrogenase. An approach based on the use of different oligomeric forms of the enzyme immobilized on sepharose

Comparative Analysis of the Effects of [alpha]-Crystallin and GroEL on the Kinetics of Thermal Aggregation of Rabbit Muscle Glyceraldehyde-3-Phosphate Dehydrogenase

Interaction of polyanions with basic proteins, 2(a) : influence of complexing polyanions on the thermo-aggregation of oligomeric enzymes

Interaction of polyanions with basic proteins, 2a Influence of complexing polyanions on the thermoaggregation of oligomeric enzymes

SH-containing compounds as allosteric effectors of glyceraldehyde-3-phosphate dehydrogenase

D-glyceraldehyde-3-phosphate dehydrogenase. Properties of the enzyme modified at arginine residues

Thermal unfolding of phosphorylating d-glyceraldehyde-3-phosphate dehydrogenase studied by differential scanning calorimetry

Rabbit muscle D-Glyceraldehyde-3-phosphate dehydrogenase: Half-of-the-sites reactivity of the enzyme modified at arginine residues

Auramine O as a Conformational Probe to Study Glyceraldehyde 3‐Phosphate Dehydrogenase

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