Balobanov V - Search Results

1

The New Functional Hybrid Chaperone Protein ADGroEL-SacSm.

Mikhaylina A, Lekontseva N, Marchenkov V, Kolesnikova V, Khairetdinova A, Nikonov O, Balobanov V. Mikhaylina A, et al. Among authors: balobanov v. Molecules. 2023 Aug 23;28(17):6196. doi: 10.3390/molecules28176196. Molecules. 2023. PMID: 37687025 Free PMC article.

2

Characterization of RNA-binding properties of the archaeal Hfq-like protein from Methanococcus jannaschii.

Nikulin A, Mikhailina A, Lekontseva N, Balobanov V, Nikonova E, Tishchenko S. Nikulin A, et al. Among authors: balobanov v. J Biomol Struct Dyn. 2017 Jun;35(8):1615-1628. doi: 10.1080/07391102.2016.1189849. Epub 2016 Aug 1. J Biomol Struct Dyn. 2017. PMID: 27187760

3

sw ApoMb Amyloid Aggregation under Nondenaturing Conditions: The Role of Native Structure Stability.

Katina NS, Balobanov VA, Ilyina NB, Vasiliev VD, Marchenkov VV, Glukhov AS, Nikulin AD, Bychkova VE. Katina NS, et al. Among authors: balobanov va. Biophys J. 2017 Sep 5;113(5):991-1001. doi: 10.1016/j.bpj.2017.07.011. Biophys J. 2017. PMID: 28877500 Free PMC article.

4

Near-Wall Aggregation of Amyloidogenic Aβ 1-40 Peptide: Direct Observation by the FRET.

Katina N, Mikhaylina A, Ilina N, Eliseeva I, Balobanov V. Katina N, et al. Among authors: balobanov v. Molecules. 2021 Dec 15;26(24):7590. doi: 10.3390/molecules26247590. Molecules. 2021. PMID: 34946672 Free PMC article.

5

The Molten Globule State of a Globular Protein in a Cell Is More or Less Frequent Case Rather than an Exception.

Bychkova VE, Dolgikh DA, Balobanov VA, Finkelstein AV. Bychkova VE, et al. Among authors: balobanov va. Molecules. 2022 Jul 7;27(14):4361. doi: 10.3390/molecules27144361. Molecules. 2022. PMID: 35889244 Free PMC article. Review.

6

Influence of Amino Acid Substitutions in ApoMb on Different Stages of Unfolding of Amyloids.

Katina N, Marchenkov V, Ryabova N, Ilyina N, Marchenko N, Balobanov V, Finkelstein A. Katina N, et al. Among authors: balobanov v. Molecules. 2023 Nov 23;28(23):7736. doi: 10.3390/molecules28237736. Molecules. 2023. PMID: 38067466 Free PMC article.

7

The Kinetics of Amyloid Fibril Formation by de Novo Protein Albebetin and Its Mutant Variants.

Balobanov V, Chertkova R, Egorova A, Dolgikh D, Bychkova V, Kirpichnikov M. Balobanov V, et al. Biomolecules. 2020 Feb 5;10(2):241. doi: 10.3390/biom10020241. Biomolecules. 2020. PMID: 32033353 Free PMC article.

8

pH-induced equilibrium unfolding of apomyoglobin: substitutions at conserved Trp14 and Met131 and non-conserved Val17 positions.

Dyuysekina AE, Dolgikh DA, Samatova Baryshnikova EN, Tiktopulo EI, Balobanov VA, Bychkova VE. Dyuysekina AE, et al. Among authors: balobanov va. Biochemistry (Mosc). 2008 Jun;73(6):693-701. doi: 10.1134/s0006297908060102. Biochemistry (Mosc). 2008. PMID: 18620536

9

Apomyoglobin mutants with single point mutations at val10 can form amyloid structures at permissive temperature.

Katina NS, Ilyina NB, Kashparov IA, Balobanov VA, Vasiliev VD, Bychkova VE. Katina NS, et al. Among authors: balobanov va. Biochemistry (Mosc). 2011 May;76(5):555-63. doi: 10.1134/S0006297911050051. Biochemistry (Mosc). 2011. PMID: 21639835

10

The Molten Globule Concept: 45 Years Later.

Bychkova VE, Semisotnov GV, Balobanov VA, Finkelstein AV. Bychkova VE, et al. Among authors: balobanov va. Biochemistry (Mosc). 2018 Jan;83(Suppl 1):S33-S47. doi: 10.1134/S0006297918140043. Biochemistry (Mosc). 2018. PMID: 29544429 Free article. Review.

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