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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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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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Peptide Aβ(16-25) forms nanofilms in the process of its aggregation

Biochemistry (Moscow), 2016-07, Vol.81 (7), p.755-761

2016

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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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Electron Microscopy of Stable Electrophoretic Fractions of Natural Humic Acids as a Key to the Understanding of Their Structural Organization

Russian journal of bioorganic chemistry, 2024, Vol.50 (3), p.766-777

2024

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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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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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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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Determination of size of folding nuclei of fibrils formed from recombinant Aβ(1-40) peptide

Biochemistry (Moscow), 2016-05, Vol.81 (5), p.538-547

2016

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S1 ribosomal protein family contains a unique conservative domain

Molecular biology (New York), 2010-08, Vol.44 (4), p.642-647

2010

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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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Loops and repeats in proteins as footprints of molecular evolution

Biochemistry (Moscow), 2012-12, Vol.77 (13), p.1487-1499

2012

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Supramolecular organization of Hfq-like proteins

Biochemistry (Moscow), 2015-04, Vol.80 (4), p.441-448

2015

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Proteolysis of ribosomal protein S1 from Escherichia coli and Thermus thermophilus leads to formation of two different fragments

Biochemistry (Moscow), 2007-11, Vol.72 (11), p.1225-1232

2007

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In vitro Assembly of a Ribonucleoprotein Particle Corresponding to the Platform Domain of the 30S Ribosomal Subunit

Proceedings of the National Academy of Sciences - PNAS, 1998-02, Vol.95 (3), p.999-1003

1998

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Amyloid Core Wild-Type Apomyoglobin and Its Mutant Variants Is Formed by Different Regions of the Polypeptide Chain

Molecular biology (New York), 2018, Vol.52 (1), p.42-51

2018

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Amyloid Core Wild-Type Apomyoglobin and Its Mutant Variants Is Formed by Different Regions of the Polypeptide Chain

Molekuliarnaia biologiia, 2018-01, Vol.52 (1), p.51

2018

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YB-1 is capable of forming extended nanofibrils

Biochemistry (Moscow), 2010, Vol.75 (1), p.115-120

2010

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Electron microscopy of stable electrophoretic fractions of natural humic acids – the key to the understanding of their structural organization

Биоорганическая химия, 2024-08, Vol.50 (3), p.324-334

2024

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Crystallins Are Small Heat Shock Proteins: Functional and Structural Properties

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

2017

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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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Does the channel for nascent peptide exist inside the ribosome? Immune electron microscopy study

FEBS letters, 1988-01, Vol.226 (2), p.255-260

1988

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Determination of Regions Involved in Amyloid Fibril Formation for A[beta] Peptide

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

2016

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Structural studies of the 30S subunit of ribosomes Thermus thermophilus by small-angle neutron and X-ray scattering

Journal of applied crystallography, 2000-06, Vol.33 (3-1), p.515-518

2000

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

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

Peptide Aβ(16-25) forms nanofilms in the process of its aggregation

Influence of Chaperones on Amyloid Formation of Аβ Peptide

Electron Microscopy of Stable Electrophoretic Fractions of Natural Humic Acids as a Key to the Understanding of Their Structural Organization

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

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

Analysis of Insulin Analogs and the Strategy of Their Further Development

Determination of size of folding nuclei of fibrils formed from recombinant Aβ(1-40) peptide

S1 ribosomal protein family contains a unique conservative domain

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

Loops and repeats in proteins as footprints of molecular evolution

Supramolecular organization of Hfq-like proteins

Proteolysis of ribosomal protein S1 from Escherichia coli and Thermus thermophilus leads to formation of two different fragments

In vitro Assembly of a Ribonucleoprotein Particle Corresponding to the Platform Domain of the 30S Ribosomal Subunit

Amyloid Core Wild-Type Apomyoglobin and Its Mutant Variants Is Formed by Different Regions of the Polypeptide Chain

Amyloid Core Wild-Type Apomyoglobin and Its Mutant Variants Is Formed by Different Regions of the Polypeptide Chain

YB-1 is capable of forming extended nanofibrils

Electron microscopy of stable electrophoretic fractions of natural humic acids – the key to the understanding of their structural organization

Crystallins Are Small Heat Shock Proteins: Functional and Structural Properties

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

Does the channel for nascent peptide exist inside the ribosome? Immune electron microscopy study

Determination of Regions Involved in Amyloid Fibril Formation for A[beta] Peptide

Structural studies of the 30S subunit of ribosomes Thermus thermophilus by small-angle neutron and X-ray scattering

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