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Radius of gyration as an indicator of protein structure compactness

Molecular biology (New York), 2008-08, Vol.42 (4), p.623-628

2008

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Identification of Amyloidogenic Regions in the Spine of Insulin Fibrils

Biochemistry (Moscow), 2019, Vol.84 (1), p.47-55

2019

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Influence of Chaperones on Amyloid Formation of Аβ Peptide

Current protein & peptide science, 2022, Vol.23 (1), p.44-51

2022

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Are the same or different amino acid residues responsible for correct and incorrect protein folding?

Biochemistry (Moscow), 2009-02, Vol.74 (2), p.186-193

Galzitskaya, O. V

2009

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Comparison of deep learning models with simple method to assess the problem of antimicrobial peptides prediction

Molecular informatics, 2024-05, Vol.43 (5), p.e202200181-n/a

2024

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Is protein folding rate dependent on number of folding stages? Modeling of protein folding with ferredoxin-like fold

Biochemistry (Moscow), 2010-06, Vol.75 (6), p.717-727

Galzitskaya, O. V

2010

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Structure and functions of syndecans in vertebrates

Biochemistry (Moscow), 2013-10, Vol.78 (10), p.1071-1085

2013

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Structural polymorphism and possible pathways of amyloid fibril formation on the example of insulin protein

Biochemistry (Moscow), 2012-11, Vol.77 (11), p.1237-1247

2012

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Studies of the Process of Amyloid Formation by Aβ Peptide

Biochemistry (Moscow), 2018, Vol.83 (Suppl 1), p.S62-S80

2018

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Structural, Functional, and Evolutionary Characteristics of Proteins with Repeats

Molecular biology (New York), 2021-09, Vol.55 (5), p.683-704

2021

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The role of β-amyloid peptide in neurodegenerative diseases

Ageing research reviews, 2011-09, Vol.10 (4), p.440-452

2011

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Comparative Analysis of Aggregation of Thermus thermophilus Ribosomal Protein bS1 and Its Stable Fragment

Biochemistry (Moscow), 2020-03, Vol.85 (3), p.344-354

2020

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Bacterial proteins fold faster than eukaryotic proteins with simple folding kinetics

Biochemistry (Moscow), 2011-02, Vol.76 (2), p.225-235

2011

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Statistical analysis of unstructured amino acid residues in protein structures

Biochemistry (Moscow), 2010-02, Vol.75 (2), p.192-200

2010

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Influence of organization of native protein structure on its folding: Modeling of the folding of α-helical proteins

Biochemistry (Moscow), 2010-08, Vol.75 (8), p.995-1005

2010

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Mechanisms of amyloid fibril formation

Biochemistry (Moscow), 2014-12, Vol.79 (13), p.1515-1527

2014

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α-Crystallins are small heat shock proteins: Functional and structural properties

Biochemistry (Moscow), 2017-02, Vol.82 (2), p.106-121

2017

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Analysis of Insulin Analogs and the Strategy of Their Further Development

Biochemistry (Moscow), 2018, Vol.83 (Suppl 1), p.S146-S162

2018

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Prediction of folding nuclei in tRNA molecules

Biochemistry (Moscow), 2011-02, Vol.76 (2), p.236-244

2011

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An Overlap between Splicing Sites in RNA and Homo-Repeats in Human Proteins

Molecular biology (New York), 2019-05, Vol.53 (3), p.470-474

2019

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Occurrence of disordered patterns and homorepeats in eukaryotic and bacterial proteomes

Molecular bioSystems, 2012-01, Vol.8 (1), p.327-337

2012

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Functionally Significant Amino Acid Motifs of Heat Shock Proteins: Structural and Bioinformatics Analyses of Hsp60/Hsp10 in Five Classes of Chordata

Molecular biology (New York), 2018-09, Vol.52 (5), p.761-778

2018

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Amyloid properties of titin

Biochemistry (Moscow), 2017-12, Vol.82 (13), p.1675-1685

2017

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Determination of regions involved in amyloid fibril formation for Aβ(1-40) peptide

Biochemistry (Moscow), 2016-07, Vol.81 (7), p.762-769

2016

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Comparison of transition states obtained upon modeling of unfolding of immunoglobulin-binding domains of proteins L and G caused by external action with transition states obtained in the absence of force probed by experiments

Biochemistry (Moscow), 2009-03, Vol.74 (3), p.316-328

2009

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Radius of gyration as an indicator of protein structure compactness

Identification of Amyloidogenic Regions in the Spine of Insulin Fibrils

Influence of Chaperones on Amyloid Formation of Аβ Peptide

Are the same or different amino acid residues responsible for correct and incorrect protein folding?

Comparison of deep learning models with simple method to assess the problem of antimicrobial peptides prediction

Is protein folding rate dependent on number of folding stages? Modeling of protein folding with ferredoxin-like fold

Structure and functions of syndecans in vertebrates

Structural polymorphism and possible pathways of amyloid fibril formation on the example of insulin protein

Studies of the Process of Amyloid Formation by Aβ Peptide

Structural, Functional, and Evolutionary Characteristics of Proteins with Repeats

The role of β-amyloid peptide in neurodegenerative diseases

Comparative Analysis of Aggregation of Thermus thermophilus Ribosomal Protein bS1 and Its Stable Fragment

Bacterial proteins fold faster than eukaryotic proteins with simple folding kinetics

Statistical analysis of unstructured amino acid residues in protein structures

Influence of organization of native protein structure on its folding: Modeling of the folding of α-helical proteins

Mechanisms of amyloid fibril formation

α-Crystallins are small heat shock proteins: Functional and structural properties

Analysis of Insulin Analogs and the Strategy of Their Further Development

Prediction of folding nuclei in tRNA molecules

An Overlap between Splicing Sites in RNA and Homo-Repeats in Human Proteins

Occurrence of disordered patterns and homorepeats in eukaryotic and bacterial proteomes

Functionally Significant Amino Acid Motifs of Heat Shock Proteins: Structural and Bioinformatics Analyses of Hsp60/Hsp10 in Five Classes of Chordata

Amyloid properties of titin

Determination of regions involved in amyloid fibril formation for Aβ(1-40) peptide

Comparison of transition states obtained upon modeling of unfolding of immunoglobulin-binding domains of proteins L and G caused by external action with transition states obtained in the absence of force probed by experiments

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