Search Results - "Selivanova, O M"

α-Crystallins are small heat shock proteins: Functional and structural properties by Tikhomirova, T. S., Selivanova, O. M., Galzitskaya, O. V.

“…During its life cycle, a cell can be subjected to various external negative effects. Many proteins provide cell protection, including small heat shock proteins…”
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Determination of regions involved in amyloid fibril formation for Aβ(1-40) peptide by Surin, A. K., Grigorashvili, E. I., Suvorina, M. Yu, Selivanova, O. M., Galzitskaya, O. V.

“…The studies of amyloid structures and the process of their formation are important problems of biophysics. One of the aspects of such studies is to determine…”
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Peptide Aβ(16-25) forms nanofilms in the process of its aggregation by Selivanova, O. M., Gorbunova, E. Yu, Mustaeva, L. G., Grigorashvili, E. I., Suvorina, M. Yu, Surin, A. K., Galzitskaya, O. V.

“…A method for the synthesis and high purification of fragments of Aβ(1-42) peptide has been elaborated. We have synthesized the amyloidogenic fragment Aβ(16-25)…”
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Electron Microscopy of Stable Electrophoretic Fractions of Natural Humic Acids as a Key to the Understanding of Their Structural Organization by Trubetskaya, O. E., Selivanova, O. M., Rogachevskii, V. V., Trubetskoj, O. A.

“…Objective: Natural humic substances (HS) make up a significant part of the organic carbon of the biosphere. Considering the numerous significant ecological…”
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Studies of the Process of Amyloid Formation by Aβ Peptide by Galzitskaya, O. V., Galushko, E. I., Selivanova, O. M.

“…Studies of the process of amyloid formation by Aβ peptide have been topical due to the critical role of this peptide in the pathogenesis of Alzheimer’s…”
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Structural polymorphism and possible pathways of amyloid fibril formation on the example of insulin protein by Selivanova, O. M., Galzitskaya, O. V.

“…In this review we analyze the main works on amyloid formation of insulin. There are many environmental factors affecting the formation of insulin amyloid…”
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Influence of Chaperones on Amyloid Formation of Аβ Peptide by Galzitskaya, O V, Selivanova, O M, Dzhus, U F, Marchenkov, V V, Suvorina, M Yu, Surin, A K

“…An extensive study of the folding and stability of proteins and their complexes has revealed a number of problems and questions that need to be answered. One…”
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S1 ribosomal protein family contains a unique conservative domain by Deryusheva, E. I, Machulin, A. V, Selivanova, O. M, Serdyuk, I. N

“…The number of amino acid residues contained in the S1 ribosomal protein of various bacteria varies in a wide range: from 111 to 863 residues in Spiroplasma…”
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Comparative Analysis of Aggregation of Thermus thermophilus Ribosomal Protein bS1 and Its Stable Fragment by Grishin, S. Yu, Dzhus, U. F., Selivanova, O. M., Balobanov, V. A., Surin, A. K., Galzitskaya, O. V.

“…Functionally important multidomain bacterial protein bS1 is the largest ribosomal protein of subunit 30S. It interacts with both mRNA and proteins and is prone…”
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Analysis of Insulin Analogs and the Strategy of Their Further Development by Selivanova, O. M., Grishin, S. Yu, Glyakina, A. V., Sadgyan, A. S., Ushakova, N. I., Galzitskaya, O. V.

“…We analyzed the structural properties of the peptide hormone insulin and described the mechanism of its physiological action, as well as effects of insulin in…”
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Ligand-Induced Reassembly of GroEL/ES Chaperone In Vitro: Visualization by Electron Microscopy by Ryabova, N. A., Selivanova, O. M., Semisotnov, G. V.

“…The products of the reassembly reaction of tetradecameric two-ring quaternary structure of GroEL chaperonin under the pressure of its heptameric co-chaperonin…”
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Determination of size of folding nuclei of fibrils formed from recombinant Aβ(1-40) peptide by Grigorashvili, E. I., Selivanova, O. M., Dovidchenko, N. V., Dzhus, U. F., Mikhailina, A. O., Suvorina, M. Yu, Marchenkov, V. V., Surin, A. K., Galzitskaya, O. V.

“…We have developed a highly efficient method for purification of the recombinant product Aβ(1-40) peptide. The concentration dependence of amyloid formation by…”
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Proteolysis of ribosomal protein S1 from Escherichia coli and Thermus thermophilus leads to formation of two different fragments by Selivanova, O M, Fedorova, Yu Yu, Serduyk, I N

“…As a result of limited tryptic proteolysis of S1 ribosomal protein (molecular mass 60 kD) from Thermus thermophilus, 25 N-terminal amino acid residues and 71…”
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In vitro Assembly of a Ribonucleoprotein Particle Corresponding to the Platform Domain of the 30S Ribosomal Subunit by Agalarov, S. C., Zheleznyakova, E. N., Selivanova, O. M., Zheleznaya, L. A., Matvienko, N. I., Vasiliev, V. D., Spirin, A. S.

“…A fragment of the 16S RNA of Thermus thermophilus corresponding to the central domain (nucleotides 547-895) has been prepared by transcription in vitro…”
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Loops and repeats in proteins as footprints of molecular evolution by Deryusheva, E. I., Selivanova, O. M., Serdyuk, I. N.

“…This review is devoted to substantiation of new characteristics for classification of living organisms. The novel view of a role of flexible regions in protein…”
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Supramolecular organization of Hfq-like proteins by Murina, V. N., Selivanova, O. M., Mikhaylina, A. O., Kazakov, A. S., Nikonova, E. Yu, Lekontseva, N. V., Tishchenko, S. V., Nikulin, A. D.

“…Bacterial Hfq proteins are structural homologs of archaeal and eukaryotic Sm/Lsm proteins, which are characterized by a 5-stranded β-sheet and an N-terminal…”
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Amyloid Core Wild-Type Apomyoglobin and Its Mutant Variants Is Formed by Different Regions of the Polypeptide Chain by Katina, N. S., Grigorashvili, E. I., Suvorina, M. Yu, Ilyina, N. B., Ryabova, N. A., Selivanova, O. M., Surin, A. K.

“…As has been recently shown, the toxicity of protein aggregates is determined by their structure. Therefore, special attention has been focused on the search…”
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Amyloid Core Wild-Type Apomyoglobin and Its Mutant Variants Is Formed by Different Regions of the Polypeptide Chain by Katina, N S, Grigorashvili, E I, Suvorina, M Yu, Ilyina, N B, Ryabova, N A, Selivanova, O M, Surin, A K

“…As has been recently shown, the toxicity of protein aggregates is determined by their structure. Therefore, special attention has been focused on the search…”
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YB-1 is capable of forming extended nanofibrils by Selivanova, O. M., Guryanov, S. G., Enin, G. A., Skabkin, M. A., Ovchinnikov, L. P., Serdyuk, I. N.

“…Here we are the first to report that multifunctional Y-box binding protein 1 (YB-1) forms extended fibrils with a diameter of 15–20 nm. The YB-1 fibrils were…”
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Does the channel for nascent peptide exist inside the ribosome? Immune electron microscopy study by Ryabova, L.A., Selivanova, O.M., Baranov, V.I., Vasiliev, V.D., Spirin, A.S.

“…MS2 phage RNA-directed synthesis of an N-terminal polypeptide of the phage coat protein on Escherichia coli 70 S ribosomes was initiated in a cell-free system…”
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