Balobanov VA - Search Results

1

Membrane-induced changes in the holomyoglobin tertiary structure: interplay with function.

Basova LV, Tiktopulo EI, Kutyshenko VP, Klenin SI, Balobanov VA, Bychkova VE. Basova LV, et al. Among authors: balobanov va. Eur Biophys J. 2014 Jul;43(6-7):317-29. doi: 10.1007/s00249-014-0964-y. Epub 2014 May 11. Eur Biophys J. 2014. PMID: 24816544

2

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

3

[Kinetics of interaction between apomyoglobin and phospholipid membrane].

Balobanov VA, Il'ina NB, Katina NS, Kashparov IA, Dolgikh DA, Bychkova VE. Balobanov VA, et al. Mol Biol (Mosk). 2010 Jul-Aug;44(4):708-17. Mol Biol (Mosk). 2010. PMID: 20873231 Russian.

4

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

5

How membrane surface affects protein structure.

Bychkova VE, Basova LV, Balobanov VA. Bychkova VE, et al. Among authors: balobanov va. Biochemistry (Mosc). 2014 Dec;79(13):1483-514. doi: 10.1134/S0006297914130045. Biochemistry (Mosc). 2014. PMID: 25749161 Free article. Review.

6

Intermediate States of Apomyoglobin: Are They Parts of the Same Area of Conformations Diagram?

Balobanov VA, Katina NS, Finkelstein AV, Bychkova VE. Balobanov VA, et al. Biochemistry (Mosc). 2017 May;82(5):625-631. doi: 10.1134/S0006297917050108. Biochemistry (Mosc). 2017. PMID: 28601072

7

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.

8

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.

9

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.

10

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.

Save citations to file

Email citations

Send citations to clipboard

Add to Collections

Add to My Bibliography

Create a file for external citation management software

Your saved search

Your RSS Feed

My NCBI Filters

Text availability

Article attribute

Article type

Publication date

21 results

Search Page