Publications by authors named "Victor Marchenkov"

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How proteins manage to fold and how chaperones manage to assist the folding.
Sergiy O Garbuzynskiy, Victor V Marchenkov, Natalia Y Marchenko, Gennady V Semisotnov, Alexei V Finkelstein

Phys Life Rev· March 2025

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Acceleration of carbonic anhydrase amyloid aggregation leads to a decrease in the fibrils toxicity.
Liliia Fakhranurova, Victor Marchenkov, Anatoly Glukhov, Vitalii Balobanov, Natalya Ryabova

Biochem Biophys Res Commun· December 2024

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Authentic hSAA related with AA amyloidosis: New method of purification, folding and amyloid polymorphism.
Natalya Katina, Victor Marchenkov, Yulia Lapteva, Vitalii Balobanov, Nelly Ilyina

Biophys Chem· October 2024

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Co-chaperonin GroES subunit exchange as dependent on time, pH, protein concentration, and urea.
Victor Marchenkov, Alexey Surin, Victor Ugarov, Nina Kotova, Natalia Marchenko

Biochim Biophys Acta Proteins Proteom· September 2024

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Bacteriophage T5 dUTPase: Combination of Common Enzymatic and Novel Functions.
Anatoly Glukhov, Victor Marchenkov, Ulyana Dzhus, Antonina Krutilina, Georgii Selikhanov

Int J Mol Sci· January 2024

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Influence of Amino Acid Substitutions in ApoMb on Different Stages of Unfolding of Amyloids.
Natalya Katina, Victor Marchenkov, Natalya Ryabova, Nelly Ilyina, Natalia Marchenko

Molecules· November 2023

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The New Functional Hybrid Chaperone Protein ADGroEL-SacSm.
Alisa Mikhaylina, Natalia Lekontseva, Victor Marchenkov, Viktoria Kolesnikova, Albina Khairetdinova

Molecules· August 2023

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In Vivo Incorporation of Photoproteins into GroEL Chaperonin Retaining Major Structural and Functional Properties.
Victor Marchenkov, Tanya Ivashina, Natalia Marchenko, Natalya Ryabova, Olga Selivanova

Molecules· February 2023

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Recombinant Globular Domain of TcpA Pilin from El Tor: Recovery from Inclusion Bodies and Structural Characterization.
Victor Marchenkov, Elena Dubovitskya, Nina Kotova, Igor Tuchkov, Nina Smirnova

Life (Basel)· November 2022

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Relationship between Changes in the Protein Folding Pathway and the Process of Amyloid Formation: The Case of Bovine Carbonic Anhydrase II.
Bogdan S Melnik, Natalya S Katina, Natalya A Ryabova, Victor V Marchenkov, Tatiana N Melnik

Int J Mol Sci· November 2022

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The Denaturant- and Mutation-Induced Disassembly of Hexameric Hfq Y55W Mutant.
Victor Marchenkov, Natalia Lekontseva, Natalia Marchenko, Ivan Kashparov, Victoriia Murina

Molecules· June 2022

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Carbonic anhydrase amyloid fibrils composed of laterally associated protofilaments show reduced cytotoxicity.
Natalya Ryabova, Liliia Fakhranurova, Vitaly Balobanov, Victor Marchenkov, Anatoly Glukhov

Biochem Biophys Res Commun· February 2022

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β-elimination of hyaluronate by red king crab hyaluronidase.
Dmitrii Sliadovskii, Tatyana Ponomareva, Maxim Molchanov, Irina Pozdnyakova-Filatova, Maria Timchenko, Victor Marchenkov

Sci Rep· November 2021

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Under Conditions of Amyloid Formation Bovine Carbonic Anhydrase B Undergoes Fragmentation by Acid Hydrolysis.
Victor Marchenkov, Natalya Ryabova, Vitaly Balobanov, Anatoly Glukhov, Nelly Ilyina

Biomolecules· October 2021

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High-performance size exclusion chromatography with online fluorescence and multi-wavelength absorbance detection for isolation of high-purity carbon dots fractions, free of non-fluorescent material.
Olga E Trubetskaya, Oleg A Trubetskoj, Claire Richard, Alexey M Vervald, Sergey A Burikov, Victor V Marchenkov

J Chromatogr A· August 2021

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The presence of cross-β-structure as a key determinant of carbonic anhydrase amyloid fibrils cytotoxicity.
Liliia Fakhranurova, Vitaly Balobanov, Natalya Ryabova, Anatoly Glukhov, Nelly Ilyina, Victor Marchenkov

Biochem Biophys Res Commun· April 2020

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Back to GroEL-Assisted Protein Folding: GroES Binding-Induced Displacement of Denatured Proteins from GroEL to Bulk Solution.
Victor Marchenkov, Andrey Gorokhovatsky, Natalia Marchenko, Tanya Ivashina, Gennady Semisotnov

Biomolecules· January 2020

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Phylogenetically Defined Isoforms of Invasion Factor InlB Differently Activate Intracellular Signaling Pathways and Interact with the Receptor gC1q-R.
Yaroslava Chalenko, Egor Kalinin, Victor Marchenkov, Elena Sysolyatina, Alexey Surin

Int J Mol Sci· August 2019

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Molecular Size Distribution of Fluorophores in Aquatic Natural Organic Matter: Application of HPSEC with Multi-Wavelength Absorption and Fluorescence Detection Following LPSEC-PAGE Fractionation.
Oleg A Trubetskoj, Claire Richard, Guillaume Voyard, Victor V Marchenkov, Olga E Trubetskaya

Environ Sci Technol· May 2018

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sw ApoMb Amyloid Aggregation under Nondenaturing Conditions: The Role of Native Structure Stability.
Natalya S Katina, Vitalii A Balobanov, Nelly B Ilyina, Victor D Vasiliev, Victor V Marchenkov

Biophys J· September 2017

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Isoforms of green fluorescent protein differ from each other in solvent molecules 'trapped' inside this protein.
Kseniya F Glukhova, Victor V Marchenkov, Tatiana N Melnik, Bogdan S Melnik

J Biomol Struct Dyn· May 2017

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X-ray diffraction and electron microscopy data for amyloid formation of Aβ40 and Aβ42.
Olga M Selivanova, Elizaveta I Grigorashvili, Mariya Yu Suvorina, Ulyana F Dzhus, Alexey D Nikulin, Victor V Marchenkov

Data Brief· September 2016

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The Mechanism Underlying Amyloid Polymorphism is Opened for Alzheimer's Disease Amyloid-β Peptide.
Olga M Selivanova, Alexey K Surin, Victor V Marchenkov, Ulyana F Dzhus, Elizaveta I Grigorashvili

J Alzheimers Dis· September 2016

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One of the possible mechanisms of amyloid fibrils formation based on the sizes of primary and secondary folding nuclei of Aβ40 and Aβ42.
Nikita V Dovidchenko, Anna V Glyakina, Olga M Selivanova, Elizaveta I Grigorashvili, Mariya Yu Suvorina, Victor V Marchenkov

J Struct Biol· June 2016

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Strict experimental evidence that apo-chaperonin GroEL does not accelerate protein folding, although it does accelerate one of its steps.
Natalia Y Marchenko, Victor V Marchenkov, Gennady V Semisotnov, Alexei V Finkelstein

Proc Natl Acad Sci U S A· December 2015

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