The molten globule concept: 45 years later VE Bychkova, GV Semisotnov, VA Balobanov, AV Finkelstein Biochemistry (Moscow) 83, S33-S47, 2018 | 38 | 2018 |
Folding intermediate and folding nucleus for I→ N and U→ I→ N transitions in apomyoglobin: contributions by conserved and nonconserved residues EN Samatova, BS Melnik, VA Balobanov, NS Katina, DA Dolgikh, ... Biophysical journal 98 (8), 1694-1702, 2010 | 30 | 2010 |
How strong are side chain interactions in the folding intermediate? EN Samatova, NS Katina, VA Balobanov, BS Melnik, DA Dolgikh, ... Protein Science 18 (10), 2152-2159, 2009 | 28 | 2009 |
Characterization of RNA-binding properties of the archaeal Hfq-like protein from Methanococcus jannaschii A Nikulin, A Mikhailina, N Lekontseva, V Balobanov, E Nikonova, ... Journal of Biomolecular Structure and Dynamics 35 (8), 1615-1628, 2017 | 22 | 2017 |
How membrane surface affects protein structure VE Bychkova, LV Basova, VA Balobanov Biochemistry (Moscow) 79, 1483-1514, 2014 | 16 | 2014 |
Intermediate states of apomyoglobin: Are they parts of the same area of conformations diagram? VA Balobanov, NS Katina, AV Finkelstein, VE Bychkova Biochemistry (Moscow) 82, 625-631, 2017 | 12 | 2017 |
Crystal structures and RNA-binding properties of Lsm proteins from archaea Sulfolobus acidocaldarius and Methanococcus vannielii: Similarity and difference of the U-binding mode N Lekontseva, A Mikhailina, M Fando, O Kravchenko, V Balobanov, ... Biochimie 175, 1-12, 2020 | 11 | 2020 |
pH-induced equilibrium unfolding of apomyoglobin: substitutions at conserved Trp14 and Met131 and non-conserved Val17 positions AE Dyuysekina, DA Dolgikh, EN Samatova, EI Tiktopulo, VA Balobanov, ... Biochemistry (Moscow) 73, 693-701, 2008 | 11 | 2008 |
Apomyoglobin mutants with single point mutations at Val10 can form amyloid structures at permissive temperature NS Katina, NB Ilyina, IA Kashparov, VA Balobanov, VD Vasiliev, ... Biochemistry (Moscow) 76, 555-563, 2011 | 10 | 2011 |
Comparative Analysis of Aggregation of Thermus thermophilus Ribosomal Protein bS1 and Its Stable Fragment SY Grishin, UF Dzhus, OM Selivanova, VA Balobanov, AK Surin, ... Biochemistry (Moscow) 85 (3), 344-354, 2020 | 9 | 2020 |
sw ApoMb amyloid aggregation under nondenaturing conditions: the role of native structure stability NS Katina, VA Balobanov, NB Ilyina, VD Vasiliev, VV Marchenkov, ... Biophysical Journal 113 (5), 991-1001, 2017 | 9 | 2017 |
An experimental tool to estimate the probability of a nucleotide presence in the crystal structures of the nucleotide–protein complexes M Nemchinova, V Balobanov, E Nikonova, N Lekontseva, A Mikhaylina, ... The Protein Journal 36, 157-165, 2017 | 8 | 2017 |
The molten globule state of a globular protein in a cell is more or less frequent case rather than an exception VE Bychkova, DA Dolgikh, VA Balobanov, AV Finkelstein Molecules 27 (14), 4361, 2022 | 7 | 2022 |
Use of fluorescent nucleotides to map RNA-binding sites on protein surface V Balobanov, N Lekontseva, A Mikhaylina, A Nikulin RNA Spectroscopy: Methods and Protocols, 251-262, 2020 | 6 | 2020 |
Loops linking secondary structure elements affect the stability of the molten globule intermediate state of apomyoglobin MA Majorina, VA Balobanov, VN Uversky, BS Melnik FEBS letters 594 (20), 3293-3304, 2020 | 5 | 2020 |
The presence of cross-β-structure as a key determinant of carbonic anhydrase amyloid fibrils cytotoxicity L Fakhranurova, V Balobanov, N Ryabova, A Glukhov, N Ilyina, ... Biochemical and Biophysical Research Communications 524 (2), 453-458, 2020 | 5 | 2020 |
The Kinetics of Amyloid Fibril Formation by de Novo Protein Albebetin and Its Mutant Variants V Balobanov, R Chertkova, A Egorova, D Dolgikh, V Bychkova, ... Biomolecules 10 (2), 241, 2020 | 5 | 2020 |
Dimerization of long hibernation promoting factor from Staphylococcus aureus: structural analysis and biochemical characterization KS Usachev, BF Fatkhullin, EA Klochkova, AK Miftakhov, AA Golubev, ... Journal of Structural Biology 209 (1), 107408, 2020 | 5 | 2020 |
Membrane-induced changes in the holomyoglobin tertiary structure: interplay with function LV Basova, EI Tiktopulo, VP Kutyshenko, SI Klenin, VA Balobanov, ... European Biophysics Journal 43, 317-329, 2014 | 4 | 2014 |
The New Functional Hybrid Chaperone Protein ADGroEL–SacSm A Mikhaylina, N Lekontseva, V Marchenkov, V Kolesnikova, ... Molecules 28 (17), 6196, 2023 | 3 | 2023 |