O. M. Selivanova

发表

The S1 ribosomal protein family contains a unique conservative domain

I. Serdyuk, A. Machulin, E. I. Deryusheva, 2010, Molecular Biology.

Taxonomic distribution, repeats, and functions of the S1 domain‐containing proteins as members of the OB‐fold family

O. Galzitskaya, A. Machulin, O. M. Selivanova, 2017, Proteins.

Antimicrobial and Amyloidogenic Activity of Peptides Synthesized on the Basis of the Ribosomal S1 Protein from Thermus Thermophilus

O. Galzitskaya, A. Surin, S. Grishin, 2020, International journal of molecular sciences.

Should the Treatment of Amyloidosis Be Personified? Molecular Mechanism of Amyloid Formation by Aβ Peptide and Its Fragments

O. Galzitskaya, A. Surin, A. Glyakina, 2018, Journal of Alzheimer's disease reports.

Identification of Amyloidogenic Regions in Pseudomonas aeruginosa Ribosomal S1 Protein

O. Galzitskaya, A. Surin, S. Grishin, 2021, International journal of molecular sciences.

How to determine the size of folding nuclei of protofibrils from the concentration dependence of the rate and lag-time of aggregation. II. Experimental application for insulin and LysPro insulin: aggregation morphology, kinetics, and sizes of nuclei.

A. V. Finkelstein, N. Dovidchenko, O. Galzitskaya, 2014, The journal of physical chemistry. B.

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

N. Dovidchenko, O. Galzitskaya, A. Surin, 2016, Biochemistry (Moscow).

Studies of Polymorphism of Amyloid-β42 Peptide from Different Suppliers.

O. Galzitskaya, A. Surin, V. Marchenkov, 2015, Journal of Alzheimer's disease : JAD.

Kinetics of Amyloid Formation by Different Proteins and Peptides: Polymorphism and Sizes of Folding Nuclei of Fibrils

N. Dovidchenko, O. Galzitskaya, O. M. Selivanova, 2016 .

Smooth muscle titin forms in vitro amyloid aggregates

N. Dovidchenko, O. Galzitskaya, Z. Podlubnaya, 2016, Bioscience reports.

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

O. Galzitskaya, O. M. Selivanova, T. Tikhomirova, 2017, Biochemistry (Moscow).

Mechanism of Amyloid Gel Formation by Several Short Amyloidogenic Peptides

O. Galzitskaya, A. Surin, O. M. Selivanova, 2021, Nanomaterials.

Different amyloid aggregation of smooth muscles titin in vitro

A. Timchenko, A. Bobylev, O. M. Selivanova, 2018, Journal of biomolecular structure & dynamics.

Structural model of amyloid fibrils for amyloidogenic peptide from Bgl2p-glucantransferase of S. cerevisiae cell wall and its modifying analog. New morphology of amyloid fibrils.

N. Dovidchenko, O. Galzitskaya, A. Surin, 2016, Biochimica et biophysica acta.

Formation of Amyloid-Like Fibrils by Y-Box Binding Protein 1 (YB-1) Is Mediated by Its Cold Shock Domain and Modulated by Disordered Terminal Domains

B. Melnik, I. Serdyuk, L. Ovchinnikov, 2012, PloS one.

Structure of protein‐deficient 50 S ribosomal subunits

A. Gudkov, O. M. Selivanova, G. Gongadze, 1986, FEBS letters.

Rosetta Stone for Amyloid Fibrils: The Key Role of Ring-Like Oligomers in Amyloidogenesis.

O. Galzitskaya, O. M. Selivanova, O. Selivanova, 2017, Journal of Alzheimer's disease : JAD.

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

O. Galzitskaya, A. Surin, O. M. Selivanova, 2016, Biochemistry (Moscow).

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

O. Galzitskaya, A. Surin, O. M. Selivanova, 2016, Biochemistry (Moscow).

Structural and Functional Peculiarities of α-Crystallin

O. Galzitskaya, O. M. Selivanova, O. Selivanova, 2020, Biology.

The Mechanism Underlying Amyloid Polymorphism is Opened for Alzheimer's Disease Amyloid-β Peptide.

N. Dovidchenko, O. Galzitskaya, A. Surin, 2016, Journal of Alzheimer's disease : JAD.

Amyloidogenic Propensities of Ribosomal S1 Proteins: Bioinformatics Screening and Experimental Checking

O. Galzitskaya, A. Surin, S. Grishin, 2020, International journal of molecular sciences.

Loops and repeats in proteins as footprints of molecular evolution

I. Serdyuk, E. I. Deryusheva, O. M. Selivanova, 2012, Biochemistry (Moscow).

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

O. Galzitskaya, O. M. Selivanova, O. Selivanova, 2012, Biochemistry (Moscow).

Strand-like structures and their three-dimensional organization in the large subunit of theEscherichia coli ribosome

E. Orlova, N. Kiselev, O. M. Selivanova, 1982, Molecular Biology Reports.

Structure of the Escherichia coli 50 S ribosomal subunit.

O. M. Selivanova, V. Vasiliev, S. Ryazantsev, 1983, Journal of molecular biology.

Fine structure of the 30 S ribosomal subunit

E. Orlova, N. Kiselev, O. M. Selivanova, 1985, FEBS letters.